Substrate recognition by complement convertases revealed in the C5-cobra venom factor complex
Complement acts as a danger‐sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases. These contain a non‐catalytic substrate contacting subunit (C3b or C4b) in complex with...
Saved in:
Published in | The EMBO journal Vol. 30; no. 3; pp. 606 - 616 |
---|---|
Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Chichester, UK
John Wiley & Sons, Ltd
02.02.2011
Blackwell Publishing Ltd Nature Publishing Group |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Complement acts as a danger‐sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases. These contain a non‐catalytic substrate contacting subunit (C3b or C4b) in complex with a protease subunit (Bb or C2a). We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution. The structures reveal a parallel two‐point attachment between C5 and CVF, where the presence of SSL7 only slightly affects the C5–CVF interface, explaining the IgA dependence for SSL7‐mediated inhibition of C5 cleavage. CVF functions as a relatively rigid binding scaffold inducing a conformational change in C5, which positions its cleavage site in proximity to the serine protease Bb. A general model for substrate recognition by the convertases is presented based on the C5–CVF and C3b–Bb–SCIN structures. Prior knowledge concerning interactions between the endogenous convertases and their substrates is rationalized by this model.
Activation of the complement system by proteolytic cleavage leads to an inflammatory response. The complement components C3 and C5 are cleaved by convertases. Here, the crystal structure of C5 in complex with cobra venom factor provides structural insight into how complement convertases recognize their substrates. |
---|---|
AbstractList | Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases. These contain a non-catalytic substrate contacting subunit (C3b or C4b) in complex with a protease subunit (Bb or C2a). We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution. The structures reveal a parallel two-point attachment between C5 and CVF, where the presence of SSL7 only slightly affects the C5-CVF interface, explaining the IgA dependence for SSL7-mediated inhibition of C5 cleavage. CVF functions as a relatively rigid binding scaffold inducing a conformational change in C5, which positions its cleavage site in proximity to the serine protease Bb. A general model for substrate recognition by the convertases is presented based on the C5-CVF and C3b-Bb-SCIN structures. Prior knowledge concerning interactions between the endogenous convertases and their substrates is rationalized by this model. Activation of the complement system by proteolytic cleavage leads to an inflammatory response. The complement components C3 and C5 are cleaved by convertases. Here, the crystal structure of C5 in complex with cobra venom factor provides structural insight into how complement convertases recognize their substrates. Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases. These contain a non-catalytic substrate contacting subunit (C3b or C4b) in complex with a protease subunit (Bb or C2a). We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution. The structures reveal a parallel two-point attachment between C5 and CVF, where the presence of SSL7 only slightly affects the C5–CVF interface, explaining the IgA dependence for SSL7-mediated inhibition of C5 cleavage. CVF functions as a relatively rigid binding scaffold inducing a conformational change in C5, which positions its cleavage site in proximity to the serine protease Bb. A general model for substrate recognition by the convertases is presented based on the C5–CVF and C3b–Bb–SCIN structures. Prior knowledge concerning interactions between the endogenous convertases and their substrates is rationalized by this model. Complement acts as a danger‐sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases. These contain a non‐catalytic substrate contacting subunit (C3b or C4b) in complex with a protease subunit (Bb or C2a). We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution. The structures reveal a parallel two‐point attachment between C5 and CVF, where the presence of SSL7 only slightly affects the C5–CVF interface, explaining the IgA dependence for SSL7‐mediated inhibition of C5 cleavage. CVF functions as a relatively rigid binding scaffold inducing a conformational change in C5, which positions its cleavage site in proximity to the serine protease Bb. A general model for substrate recognition by the convertases is presented based on the C5–CVF and C3b–Bb–SCIN structures. Prior knowledge concerning interactions between the endogenous convertases and their substrates is rationalized by this model. Activation of the complement system by proteolytic cleavage leads to an inflammatory response. The complement components C3 and C5 are cleaved by convertases. Here, the crystal structure of C5 in complex with cobra venom factor provides structural insight into how complement convertases recognize their substrates. Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases. These contain a non-catalytic substrate contacting subunit (C3b or C4b) in complex with a protease subunit (Bb or C2a). We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution. The structures reveal a parallel two-point attachment between C5 and CVF, where the presence of SSL7 only slightly affects the C5-CVF interface, explaining the IgA dependence for SSL7-mediated inhibition of C5 cleavage. CVF functions as a relatively rigid binding scaffold inducing a conformational change in C5, which positions its cleavage site in proximity to the serine protease Bb. A general model for substrate recognition by the convertases is presented based on the C5-CVF and C3b-Bb-SCIN structures. Prior knowledge concerning interactions between the endogenous convertases and their substrates is rationalized by this model. [PUBLICATION ABSTRACT] |
Author | Braren, Ingke Andersen, Kasper R Sottrup-Jensen, Lars Spillner, Edzard Andersen, Gregers R Laursen, Nick S |
Author_xml | – sequence: 1 givenname: Nick S surname: Laursen fullname: Laursen, Nick S organization: Department of Molecular Biology, Aarhus University, Aarhus, Denmark – sequence: 2 givenname: Kasper R surname: Andersen fullname: Andersen, Kasper R organization: Department of Molecular Biology, Aarhus University, Aarhus, Denmark – sequence: 3 givenname: Ingke surname: Braren fullname: Braren, Ingke organization: Institute of Biochemistry and Molecular Biology, Department of Chemistry, University of Hamburg, Hamburg, Germany – sequence: 4 givenname: Edzard surname: Spillner fullname: Spillner, Edzard organization: Institute of Biochemistry and Molecular Biology, Department of Chemistry, University of Hamburg, Hamburg, Germany – sequence: 5 givenname: Lars surname: Sottrup-Jensen fullname: Sottrup-Jensen, Lars organization: Department of Molecular Biology, Aarhus University, Aarhus, Denmark – sequence: 6 givenname: Gregers R surname: Andersen fullname: Andersen, Gregers R email: gra@mb.au.dk organization: Department of Molecular Biology, Aarhus University, Aarhus, Denmark |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21217642$$D View this record in MEDLINE/PubMed |
BookMark | eNpdkc1v1DAQxS1URLeFK0cUceGUMmM7iXNBgqUtH6UcAHFCluNM2iyJvTjJtvvf4-0uW-DkGc1vnp_9jtiB844Ye4pwgiDUS-orvzjhEHsh8QGbocwh5VBkB2wGPMdUoioP2dEwLAAgUwU-YoccORa55DP248tUDWMwIyWBrL9y7dh6l1TrxPp-2VFPboylW1EYzUBDpFZkOqqT1iXjNSXzLLW-CiZZkfN90hg7-rBbvn3MHjamG-jJ7jxm385Ov87fpRefz9_PX1-kNsuiRYOIErmxNZicK0kFgirrumlMwzMLDdgSOQfAJlMC6iYvsSwsr5VqpEEhjtmrre5yqnqqbTQdTKeXoe1NWGtvWv3vxLXX-sqvtAAhAWUUeLETCP7XRMOo-3aw1HXGkZ8GrWQJoDKFkXz-H7nwU3DxdRFSBYDIN3LP_vazN_Ln3yNQbIGbtqP1fo6gN6nqu1T1JlUdU9Wnn9582DSxvr_fmXEKtF-9W7mH0i3UDiPd7hkTfuq8EEWmv1-eaz4v315y_Ki5-A3AqbMk |
CODEN | EMJODG |
CitedBy_id | crossref_primary_10_1056_NEJMoa1311084 crossref_primary_10_3389_fimmu_2015_00262 crossref_primary_10_1016_j_molimm_2011_04_004 crossref_primary_10_1038_srep31365 crossref_primary_10_1074_jbc_M112_361121 crossref_primary_10_1038_nrneph_2012_214 crossref_primary_10_3390_v15061343 crossref_primary_10_1074_jbc_RA118_004043 crossref_primary_10_1182_blood_2020005959 crossref_primary_10_1016_j_jbc_2023_104956 crossref_primary_10_4049_jimmunol_1600280 crossref_primary_10_1016_j_toxicon_2012_05_004 crossref_primary_10_1111_imr_12465 crossref_primary_10_1111_imr_12500 crossref_primary_10_4049_jimmunol_1601932 crossref_primary_10_3389_fphy_2018_00130 crossref_primary_10_1016_j_imbio_2012_07_005 crossref_primary_10_1074_jbc_RA117_001179 crossref_primary_10_15252_embj_201899852 crossref_primary_10_3390_toxins12110669 crossref_primary_10_3389_fimmu_2018_02822 crossref_primary_10_1107_S2053230X14006967 crossref_primary_10_1002_eji_201646758 crossref_primary_10_1038_icb_2013_28 crossref_primary_10_1038_nsmb_3196 crossref_primary_10_1107_S2059798317013171 crossref_primary_10_4049_jimmunol_1402781 crossref_primary_10_1016_j_jim_2017_07_010 crossref_primary_10_1073_pnas_1909973116 crossref_primary_10_1074_jbc_RA119_012339 crossref_primary_10_1111_imr_13147 crossref_primary_10_1016_j_sbi_2012_04_001 crossref_primary_10_3389_fimmu_2018_01691 crossref_primary_10_3390_molecules27010210 crossref_primary_10_1016_j_imbio_2012_07_016 crossref_primary_10_3390_biom11020298 crossref_primary_10_1016_j_smim_2022_101627 crossref_primary_10_4049_jimmunol_2000752 crossref_primary_10_1038_s41589_019_0303_9 crossref_primary_10_3389_fimmu_2021_615748 crossref_primary_10_1016_j_csbj_2023_02_002 crossref_primary_10_1016_j_molimm_2023_12_004 crossref_primary_10_1073_pnas_1208031109 crossref_primary_10_15252_embj_201591881 crossref_primary_10_3389_fimmu_2023_1213920 crossref_primary_10_4049_jimmunol_2300128 crossref_primary_10_1016_j_molimm_2011_04_014 crossref_primary_10_1002_pro_2200 crossref_primary_10_1182_blood_2014_10_609073 crossref_primary_10_1074_jbc_M116_722017 crossref_primary_10_1007_s00281_017_0643_z crossref_primary_10_1002_1873_3468_13590 crossref_primary_10_4049_jimmunol_1500087 crossref_primary_10_1016_j_molimm_2016_07_016 crossref_primary_10_7554_eLife_63586 crossref_primary_10_1111_imr_13164 crossref_primary_10_1186_s12915_015_0203_8 crossref_primary_10_1126_science_aar5140 |
ContentType | Journal Article |
Copyright | Copyright © 2011 European Molecular Biology Organization Copyright Nature Publishing Group Feb 2, 2011 Copyright © 2011, European Molecular Biology Organization 2011 European Molecular Biology Organization |
Copyright_xml | – notice: Copyright © 2011 European Molecular Biology Organization – notice: Copyright Nature Publishing Group Feb 2, 2011 – notice: Copyright © 2011, European Molecular Biology Organization 2011 European Molecular Biology Organization |
DBID | BSCLL CGR CUY CVF ECM EIF NPM 3V. 7QG 7QL 7QP 7T5 7TK 7TM 7TO 7U9 7X7 7XB 88A 88E 8AO 8C1 8FD 8FE 8FH 8FI 8FJ 8FK 8G5 ABUWG AFKRA AZQEC BBNVY BENPR BHPHI BKSAR C1K CCPQU DWQXO FR3 FYUFA GHDGH GNUQQ GUQSH H94 HCIFZ K9. LK8 M0S M1P M2O M7N M7P MBDVC P64 PCBAR PQEST PQQKQ PQUKI PRINS Q9U RC3 7X8 5PM |
DOI | 10.1038/emboj.2010.341 |
DatabaseName | Istex Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed ProQuest Central (Corporate) Animal Behavior Abstracts Bacteriology Abstracts (Microbiology B) Calcium & Calcified Tissue Abstracts Immunology Abstracts Neurosciences Abstracts Nucleic Acids Abstracts Oncogenes and Growth Factors Abstracts Virology and AIDS Abstracts Health & Medical Collection ProQuest Central (purchase pre-March 2016) Biology Database (Alumni Edition) Medical Database (Alumni Edition) ProQuest Pharma Collection Public Health Database Technology Research Database ProQuest SciTech Collection ProQuest Natural Science Collection Hospital Premium Collection Hospital Premium Collection (Alumni Edition) ProQuest Central (Alumni) (purchase pre-March 2016) Research Library (Alumni Edition) ProQuest Central (Alumni) ProQuest Central ProQuest Central Essentials Biological Science Collection ProQuest Central Natural Science Collection Earth, Atmospheric & Aquatic Science Collection Environmental Sciences and Pollution Management ProQuest One Community College ProQuest Central Engineering Research Database Health Research Premium Collection Health Research Premium Collection (Alumni) ProQuest Central Student Research Library Prep AIDS and Cancer Research Abstracts SciTech Premium Collection ProQuest Health & Medical Complete (Alumni) Biological Sciences Health & Medical Collection (Alumni Edition) PML(ProQuest Medical Library) Research Library Algology Mycology and Protozoology Abstracts (Microbiology C) Biological Science Database Research Library (Corporate) Biotechnology and BioEngineering Abstracts Earth, Atmospheric & Aquatic Science Database ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Academic ProQuest One Academic UKI Edition ProQuest Central China ProQuest Central Basic Genetics Abstracts MEDLINE - Academic PubMed Central (Full Participant titles) |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) Research Library Prep ProQuest Central Student Oncogenes and Growth Factors Abstracts ProQuest Central Essentials Nucleic Acids Abstracts SciTech Premium Collection ProQuest Central China Environmental Sciences and Pollution Management Health Research Premium Collection Natural Science Collection Biological Science Collection ProQuest Medical Library (Alumni) Virology and AIDS Abstracts ProQuest Biological Science Collection ProQuest One Academic Eastern Edition Earth, Atmospheric & Aquatic Science Database ProQuest Hospital Collection Health Research Premium Collection (Alumni) Biological Science Database Neurosciences Abstracts ProQuest Hospital Collection (Alumni) Biotechnology and BioEngineering Abstracts ProQuest Health & Medical Complete ProQuest One Academic UKI Edition Engineering Research Database ProQuest One Academic Calcium & Calcified Tissue Abstracts Technology Research Database ProQuest Health & Medical Complete (Alumni) ProQuest Central (Alumni Edition) ProQuest One Community College Research Library (Alumni Edition) ProQuest Natural Science Collection ProQuest Pharma Collection ProQuest Biology Journals (Alumni Edition) ProQuest Central Earth, Atmospheric & Aquatic Science Collection Genetics Abstracts Health and Medicine Complete (Alumni Edition) ProQuest Central Korea Bacteriology Abstracts (Microbiology B) Algology Mycology and Protozoology Abstracts (Microbiology C) AIDS and Cancer Research Abstracts ProQuest Research Library ProQuest Public Health ProQuest Central Basic ProQuest SciTech Collection ProQuest Medical Library Animal Behavior Abstracts Immunology Abstracts ProQuest Central (Alumni) MEDLINE - Academic |
DatabaseTitleList | MEDLINE Research Library Prep |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database – sequence: 3 dbid: BENPR name: ProQuest Central url: https://www.proquest.com/central sourceTypes: Aggregation Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Chemistry Biology |
DocumentTitleAlternate | Structure of the C5–CVF complex |
EISSN | 1460-2075 |
EndPage | 616 |
ExternalDocumentID | 2255087381 21217642 EMBJ2010341 emboj2010341 ark_67375_WNG_2C9DN21K_2 |
Genre | article Research Support, Non-U.S. Gov't Journal Article |
GroupedDBID | --- -DZ -Q- -~X 0R~ 123 1OC 24P 29G 2WC 33P 36B 39C 3V. 4.4 53G 5VS 70F 7X7 88A 88E 8AO 8C1 8CJ 8FE 8FH 8FI 8FJ 8G5 8R4 8R5 A8Z AAESR AAEVG AAHHS AAIHA AAJUZ AANLZ AASGY AAXRX AAZKR ABCUV ABCVL ABHUG ABJNI ABLJU ABPTK ABUWG ABZEH ACAHQ ACBWZ ACCFJ ACCZN ACGFO ACGFS ACNCT ACPOU ACPRK ACXBN ACXME ACXQS ADAWD ADBBV ADDAD ADEOM ADKYN ADMGS ADOZA ADXAS ADZMN AEEZP AEGXH AEIGN AENEX AEQDE AEUQT AEUYR AFBPY AFFNX AFGKR AFKRA AFPWT AFRAH AFVGU AFZJQ AGJLS AHMBA AIAGR AIURR AIWBW AJBDE ALAGY ALMA_UNASSIGNED_HOLDINGS ALUQN AMBMR AMYDB AOIJS ASPBG AUFTA AVWKF AZFZN AZQEC AZVAB BAWUL BBNVY BDRZF BENPR BFHJK BHPHI BKSAR BMNLL BMXJE BPHCQ BRXPI BSCLL BTFSW BVXVI C1A CAG CCPQU COF CS3 D1J DCZOG DIK DPXWK DRFUL DRSTM DU5 DWQXO E3Z EBD EBS EJD EMB EMOBN ESTFP F5P FEDTE FYUFA G-S GNUQQ GODZA GUQSH GX1 HCIFZ HH5 HK~ HMCUK HVGLF HYE KQ8 LATKE LEEKS LH4 LITHE LK8 LOXES LUTES LW6 LYRES M0L M1P M2O M7P MEWTI MRFUL MRSTM MSFUL MSSTM MVM MXFUL MXSTM MY~ O9- OK1 P2P P2W PCBAR PQQKQ PROAC PSQYO Q2X RHF RHI RNS ROL RPM SV3 TN5 TR2 UKHRP WBKPD WH7 WIH WIK WOHZO WXSBR WYJ XFK YSK ZA5 ZCA ZZTAW ~KM - 0R ABFLS ADACO BBAFP DZ H13 HK KM MY PADUT PQEST PQUKI PRINS Q- RIG SUPJJ WIN X AAHBH ACSMW ALIPV C6C EBLON GROUPED_DOAJ CGR CUY CVF ECM EIF NPM 7QG 7QL 7QP 7T5 7TK 7TM 7TO 7U9 7XB 8FD 8FK C1K FR3 H94 K9. M7N MBDVC P64 Q9U RC3 7X8 5PM |
ID | FETCH-LOGICAL-c5561-a111412acd0a6284e71089ddffaf25c0f0c9122001f5830df69197c2d88f4a133 |
IEDL.DBID | RPM |
ISSN | 0261-4189 |
IngestDate | Tue Sep 17 21:01:54 EDT 2024 Sat Aug 17 01:21:40 EDT 2024 Fri Sep 13 00:37:27 EDT 2024 Sat Sep 28 07:57:44 EDT 2024 Sat Aug 24 00:52:09 EDT 2024 Thu Oct 07 19:36:18 EDT 2021 Wed Jan 17 05:01:17 EST 2024 |
IsDoiOpenAccess | false |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 3 |
Language | English |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c5561-a111412acd0a6284e71089ddffaf25c0f0c9122001f5830df69197c2d88f4a133 |
Notes | ArticleID:EMBJ2010341 Supplementary Animation 1Supplementary Animation 2Supplementary DataReview Process File istex:BBB50F7F2ED8D63301BB9936E1393AA47D41D86C ark:/67375/WNG-2C9DN21K-2 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
OpenAccessLink | https://doi.org/10.1038/emboj.2010.341 |
PMID | 21217642 |
PQID | 848700364 |
PQPubID | 35985 |
PageCount | 11 |
ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_3034014 proquest_miscellaneous_849008581 proquest_journals_848700364 pubmed_primary_21217642 wiley_primary_10_1038_emboj_2010_341_EMBJ2010341 nature_primary_emboj2010341 istex_primary_ark_67375_WNG_2C9DN21K_2 |
ProviderPackageCode | -Q- 70F |
PublicationCentury | 2000 |
PublicationDate | February 2, 2011 |
PublicationDateYYYYMMDD | 2011-02-02 |
PublicationDate_xml | – month: 02 year: 2011 text: February 2, 2011 day: 02 |
PublicationDecade | 2010 |
PublicationPlace | Chichester, UK |
PublicationPlace_xml | – name: Chichester, UK – name: England – name: Heidelberg |
PublicationTitle | The EMBO journal |
PublicationTitleAlternate | EMBO J |
PublicationYear | 2011 |
Publisher | John Wiley & Sons, Ltd Blackwell Publishing Ltd Nature Publishing Group |
Publisher_xml | – name: John Wiley & Sons, Ltd – name: Blackwell Publishing Ltd – name: Nature Publishing Group |
References | Cook WJ, Galakatos N, Boyar WC, Walter RL, Ealick SE (2010) Structure of human desArg-C5a. Acta Crystallogr D Biol Crystallogr 66: 190-197 Baker NA, Sept D, Joseph S, Holst MJ, McCammon JA (2001) Electrostatics of nanosystems: application to microtubules and the ribosome. Proc Natl Acad Sci USA 98: 10037-10041 Cowtan K (1994) 'Dm': an automated procedure for phase improvement by density modification. Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography 31: 34-38 Fredslund F, Laursen NS, Roversi P, Jenner L, Oliveira CL, Pedersen JS, Nunn MA, Lea SM, Discipio R, Sottrup-Jensen L, Andersen GR (2008) Structure of and influence of a tick complement inhibitor on human complement component 5. Nat Immunol 9: 753-760 Katschke Jr KJ, Stawicki S, Yin J, Steffek M, Xi H, Sturgeon L, Hass PE, Loyet KM, Deforge L, Wu Y, van Lookeren Campagne M, Wiesmann C (2009) Structural and functional analysis of a C3b-specific antibody that selectively inhibits the alternative pathway of complement. J Biol Chem 284: 10473-10479 Walport MJ (2001) Complement. First of two parts. N Engl J Med 344: 1058-1066 Sfyroera G, Ricklin D, Chen H, Nilsson-Ekdahl K, Nilsson B, Wu EL, Kaznessis YN, Lambris JD (2010) Impaired ability of complement activation via the alternative pathway C3 convertase caused by a single-point mutation in the beta chain of C3. Mol Immunol 47: 2289-2289 Kinoshita T, Takata Y, Kozono H, Takeda J, Hong KS, Inoue K (1988) C5 convertase of the alternative complement pathway: covalent linkage between two C3b molecules within the trimolecular complex enzyme. J Immunol 141: 3895-3901 Laursen NS, Gordon N, Hermans S, Lorenz N, Jackson N, Wines B, Spillner E, Christensen JB, Jensen M, Fredslund F, Bjerre M, Sottrup-Jensen L, Fraser JD, Andersen GR (2010) Structural basis for inhibition of complement C5 by the SSL7 protein from Staphylococcus aureus. Proc Natl Acad Sci USA 107: 3681-3686 Geisbrecht BV (2008) Staphylococcal complement inhibitors: biological functions, recognition of complement components, and potential therapeutic implications. Adv Exp Med Biol 632: 221-236 Janssen BJ, Gomes L, Koning RI, Svergun DI, Koster AJ, Fritzinger DC, Vogel CW, Gros P (2009) Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex. EMBO J 28: 2469-2478 Takata Y, Kinoshita T, Kozono H, Takeda J, Tanaka E, Hong K, Inoue K (1987) Covalent association of C3b with C4b within C5 convertase of the classical complement pathway. J Exp Med 165: 1494-1507 Dolinsky TJ, Nielsen JE, McCammon JA, Baker NA (2004) PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res 32: W665-W667 Wiesmann C, Katschke KJ, Yin J, Helmy KY, Steffek M, Fairbrother WJ, McCallum SA, Embuscado L, DeForge L, Hass PE, van Lookeren Campagne M (2006) Structure of C3b in complex with CRIg gives insights into regulation of complement activation. Nature 444: 217-220 Laskowski RA, MacArthur MW, Moss D, Thornton JM (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26: 283-291 Krissinel E, Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797 Martinez-Barricarte R, Heurich M, Valdes-Canedo F, Vazquez-Martul E, Torreira E, Montes T, Tortajada A, Pinto S, Lopez-Trascasa M, Morgan BP, Llorca O, Harris CL, Rodriguez de Cordoba S (2010) Human C3 mutation reveals a mechanism of dense deposit disease pathogenesis and provides insights into complement activation and regulation. J Clin Invest 120: 3702-3712 Ramsland PA, Willoughby N, Trist HM, Farrugia W, Hogarth PM, Fraser JD, Wines BD (2007) Structural basis for evasion of IgA immunity by Staphylococcus aureus revealed in the complex of SSL7 with Fc of human IgA1. Proc Natl Acad Sci USA 104: 15051-15056 DeLano WL (2002) The PyMOL User's Manual. San Carlos, CA, USA: DeLano Scientific Ebanks RO, Isenman DE (1995) Evidence for the involvement of arginine 462 and the flanking sequence of human C4 beta-chain in mediating C5 binding to the C4b subcomponent of the classical complement pathway C5 convertase. J Immunol 154: 2808-2820 Janssen BJ, Christodoulidou A, McCarthy A, Lambris JD, Gros P (2006) Structure of C3b reveals conformational changes that underlie complement activity. Nature 444: 213-216 Pangburn MK, Muller-Eberhard HJ (1983) Initiation of the alternative complement pathway due to spontaneous hydrolysis of the thioester of C3. Ann NY Acad Sci 421: 291-298 Jones TA, Cowan S, Zou J-Y, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst A 47: 110-119 Pangburn MK, Schreiber RD, Muller-Eberhard HJ (1981) Formation of the initial C3 convertase of the alternative complement pathway. Acquisition of C3b-like activities by spontaneous hydrolysis of the putative thioester in native C3. J Exp Med 154: 856-867 Kabsch W (2001) XDS. In International Tables for Crystallography, Crystallography of Biological Macromolecules, Rossmann MG, Arnold E (eds), Vol. F, p Chapter 25.22.29. Dordrecht: Kluwer Academic Publishers Kim YU, Carroll MC, Isenman DE, Nonaka M, Pramoonjago P, Takeda J, Inoue K, Kinoshita T (1992) Covalent binding of C3b to C4b within the classical complement pathway C5 convertase. Determination of amino acid residues involved in ester linkage formation. J Biol Chem 267: 4171-4176 Adams PD, Grosse-Kunstleve RW, Hung LW, Ioerger TR, McCoy AJ, Moriarty NW, Read RJ, Sacchettini JC, Sauter NK, Terwilliger TC (2002) PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr D Biol Crystallogr 58: 1948-1954 Rooijakkers SH, Wu J, Ruyken M, van Domselaar R, Planken KL, Tzekou A, Ricklin D, Lambris JD, Janssen BJ, van Strijp JA, Gros P (2009) Structural and functional implications of the alternative complement pathway C3 convertase stabilized by a staphylococcal inhibitor. Nat Immunol 10: 728-733 Vogel CW, Fritzinger DC (2010) Cobra venom factor: structure, function, and humanization for therapeutic complement depletion. Toxicon 56: 1198-1222 Gasque P (2004) Complement: a unique innate immune sensor for danger signals. Mol Immunol 41: 1089-1098 Sandoval A, Ai R, Ostresh JM, Ogata RT (2000) Distal recognition site for classical pathway convertase located in the C345C/netrin module of complement component C5. J Immunol 165: 1066-1073 Krishnan V, Ponnuraj K, Xu Y, Macon K, Volanakis JE, Narayana SV (2009) The crystal structure of cobra venom factor, a cofactor for C3- and C5-convertase CVFBb. Structure 17: 611-619 Janssen BJ, Halff EF, Lambris JD, Gros P (2007) Structure of compstatin in complex with complement component C3c reveals a new mechanism of complement inhibition. J Biol Chem 282: 29241-29247 Bestebroer J, Aerts PC, Rooijakkers SH, Pandey MK, Kohl J, van Strijp JA, de Haas CJ (2010) Functional basis for complement evasion by staphylococcal superantigen-like 7. Cell Microbiol 12: 1506-1516 Rawal N, Rajagopalan R, Salvi VP (2008) Activation of complement component C5: comparison of C5 convertases of the lectin pathway and the classical pathway of complement. J Biol Chem 283: 7853-7863 Kleywegt GJ, Jones TA (1994) Halloween... masks and bones. In From First Map to Final Model, Bailey S, Hubbard R, Waller D (eds), pp 59-66. Warrington: SERC Daresbury Laboratory Rawal N, Pangburn MK (2000) Functional role of the noncatalytic subunit of complement C5 convertase. J Immunol 164: 1379-1385 Low PJ, Ai R, Ogata RT (1999) Active sites in complement components C5 and C3 identified by proximity to indels in the C3/4/5 protein family. J Immunol 162: 6580-6588 Wu J, Wu YQ, Ricklin D, Janssen BJ, Lambris JD, Gros P (2009) Structure of complement fragment C3b-factor H and implications for host protection by complement regulators. Nat Immunol 10: 728-733 Janssen BJ, Huizinga EG, Raaijmakers HC, Roos A, Daha MR, Nilsson-Ekdahl K, Nilsson B, Gros P (2005) Structures of complement component C3 provide insights into the function and evolution of immunity. Nature 437: 505-511 Rother RP, Rollins SA, Mojcik CF, Brodsky RA, Bell L (2007) Discovery and development of the complement inhibitor eculizumab for the treatment of paroxysmal nocturnal hemoglobinuria. Nat Biotechnol 25: 1256-1264 Adcock SA, McCammon JA (2006) Molecular dynamics: survey of methods for simulating the activity of proteins. Chem Rev 106: 1589-1615 Langley R, Wines B, Willoughby N, Basu I, Proft T, Fraser JD (2005) The staphylococcal superantigen-like protein 7 binds IgA and complement C5 and inhibits IgA-Fc alpha RI binding and serum killing of bacteria. J Immunol 174: 2926-2933 Hadders MA, Pangburn MK, Svergun DI, Gros P (2010) Structural insights into the initiation of the terminal pathway. Mol Immunol 47: 2257-2258 Law SK, Dodds AW (1997) The internal thioester and the covalent binding properties of the complement proteins C3 and C4. Protein Sci 6: 263-274 Torreira E, Tortajada A, Montes T, Rodriguez de Cordoba S, Llorca O (2009) 3D structure of the C3bB complex provides insights into the activation and regulation of the complement alternative pathway convertase. Proc Natl Acad Sci USA 106: 882-887 Fredslund F, Jenner L, Husted LB, Nyborg J, Andersen GR, Sottrup-Jensen L (2006) The structure of bovine complement component 3 reveals the basis for thioester function. J Mol Biol 361: 115-127 Pangburn MK, Rawal N (2002) Structure and function of complement C5 convertase enzymes. Biochem Soc Trans 30: 1006-1010 Hayward S, Berendsen HJ (1998) Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme. Proteins 30: 144-154 Torreira, E, Tortajada, A, Montes, T, Rodriguez de Cordoba, S, Llorca, O (b45) 2009; 106 Adams, PD, Grosse-Kunstleve, RW, Hung, LW, Ioerger, TR, McCoy, AJ, Moriarty, NW, Read, RJ, Sacchettini, JC, Sauter, NK, Terwilliger, TC (b1) 2002; 58 Gasque, P (b12) 2004; 41 Fredslund, F, Laursen, NS, Roversi, P, Jenner, L, Oliveira, CL, Pedersen, JS, Nunn, MA, Lea, SM, Discipio, R, Sottrup-Jensen, L, Andersen, GR (b11) 2008; 9 Krishnan, V, Ponnuraj, K, Xu, Y, Macon, K, Volanakis, JE, Narayana, SV (b26) 2009; 17 Hadders, MA, Pangburn, MK, Svergun, DI, Gros, P (b14) 2010; 47 Hayward, S, Berendsen, HJ (b15) 1998; 30 Kim, YU, Carroll, MC, Isenman, DE, Nonaka, M, Pramoonjago, P, Takeda, J, Inoue, K, Kinoshita, T (b23) 1992; 267 Fredslund, F, Jenner, L, Husted, LB, Nyborg, J, Andersen, GR, Sottrup-Jensen, L (b10) 2006; 361 Kleywegt, GJ, Jones, TA (b25) 1994 Janssen, BJ, Gomes, L, Koning, RI, Svergun, DI, Koster, AJ, Fritzinger, DC, Vogel, CW, Gros, P (b17) 2009; 28 Laskowski, RA, MacArthur, MW, Moss, D, Thornton, JM (b29) 1993; 26 Janssen, BJ, Huizinga, EG, Raaijmakers, HC, Roos, A, Daha, MR, Nilsson-Ekdahl, K, Nilsson, B, Gros, P (b19) 2005; 437 Kinoshita, T, Takata, Y, Kozono, H, Takeda, J, Hong, KS, Inoue, K (b24) 1988; 141 Langley, R, Wines, B, Willoughby, N, Basu, I, Proft, T, Fraser, JD (b28) 2005; 174 Rawal, N, Pangburn, MK (b38) 2000; 164 Katschke, KJ, Stawicki, S, Yin, J, Steffek, M, Xi, H, Sturgeon, L, Hass, PE, Loyet, KM, Deforge, L, Wu, Y, van Lookeren Campagne, M, Wiesmann, C (b22) 2009; 284 Geisbrecht, BV (b13) 2008; 632 Jones, TA, Cowan, S, Zou, J-Y, Kjeldgaard, M (b20) 1991; 47 Ramsland, PA, Willoughby, N, Trist, HM, Farrugia, W, Hogarth, PM, Fraser, JD, Wines, BD (b37) 2007; 104 Sfyroera, G, Ricklin, D, Chen, H, Nilsson-Ekdahl, K, Nilsson, B, Wu, EL, Kaznessis, YN, Lambris, JD (b43) 2010; 47 Krissinel, E, Henrick, K (b27) 2007; 372 Pangburn, MK, Muller-Eberhard, HJ (b34) 1983; 421 Law, SK, Dodds, AW (b31) 1997; 6 Pangburn, MK, Rawal, N (b35) 2002; 30 Wu, J, Wu, YQ, Ricklin, D, Janssen, BJ, Lambris, JD, Gros, P (b49) 2009; 10 Laursen, NS, Gordon, N, Hermans, S, Lorenz, N, Jackson, N, Wines, B, Spillner, E, Christensen, JB, Jensen, M, Fredslund, F, Bjerre, M, Sottrup-Jensen, L, Fraser, JD, Andersen, GR (b30) 2010; 107 Baker, NA, Sept, D, Joseph, S, Holst, MJ, McCammon, JA (b3) 2001; 98 Takata, Y, Kinoshita, T, Kozono, H, Takeda, J, Tanaka, E, Hong, K, Inoue, K (b44) 1987; 165 Adcock, SA, McCammon, JA (b2) 2006; 106 Sandoval, A, Ai, R, Ostresh, JM, Ogata, RT (b42) 2000; 165 Janssen, BJ, Christodoulidou, A, McCarthy, A, Lambris, JD, Gros, P (b16) 2006; 444 Walport, MJ (b47) 2001; 344 Cook, WJ, Galakatos, N, Boyar, WC, Walter, RL, Ealick, SE (b5) 2010; 66 DeLano, WL (b7) 2002 Martinez-Barricarte, R, Heurich, M, Valdes-Canedo, F, Vazquez-Martul, E, Torreira, E, Montes, T, Tortajada, A, Pinto, S, Lopez-Trascasa, M, Morgan, BP, Llorca, O, Harris, CL, Rodriguez de Cordoba, S (b33) 2010; 120 Ebanks, RO, Isenman, DE (b9) 1995; 154 Wiesmann, C, Katschke, KJ, Yin, J, Helmy, KY, Steffek, M, Fairbrother, WJ, McCallum, SA, Embuscado, L, DeForge, L, Hass, PE, van Lookeren Campagne, M (b48) 2006; 444 Janssen, BJ, Halff, EF, Lambris, JD, Gros, P (b18) 2007; 282 Cowtan, K (b6) 1994; 31 Pangburn, MK, Schreiber, RD, Muller-Eberhard, HJ (b36) 1981; 154 Dolinsky, TJ, Nielsen, JE, McCammon, JA, Baker, NA (b8) 2004; 32 Kabsch, W (b21) 2001 Vogel, CW, Fritzinger, DC (b46) 2010; 56 Rother, RP, Rollins, SA, Mojcik, CF, Brodsky, RA, Bell, L (b41) 2007; 25 Bestebroer, J, Aerts, PC, Rooijakkers, SH, Pandey, MK, Kohl, J, van Strijp, JA, de Haas, CJ (b4) 2010; 12 Rawal, N, Rajagopalan, R, Salvi, VP (b39) 2008; 283 Low, PJ, Ai, R, Ogata, RT (b32) 1999; 162 Rooijakkers, SH, Wu, J, Ruyken, M, van Domselaar, R, Planken, KL, Tzekou, A, Ricklin, D, Lambris, JD, Janssen, BJ, van Strijp, JA, Gros, P (b40) 2009; 10 2010; 12 1993; 26 2010; 56 2007; 104 2002; 58 2004; 41 2001; 344 2005; 174 1987; 165 2007; 282 2010; 107 2002; 30 1992; 267 2008; 9 2005; 437 1999; 162 2010; 120 1994 1988; 141 2002 1995; 154 1997; 6 2008; 283 2009; 28 2004; 32 2010; 66 1983; 421 2010; 47 1991; 47 2009; 10 2001 2007; 372 1981; 154 2006; 361 2000; 164 2008; 632 2000; 165 2009; 284 1998; 30 2006; 106 2007; 25 2006; 444 2001; 98 1994; 31 2009; 17 2009; 106 19136636 - Proc Natl Acad Sci U S A. 2009 Jan 20;106(3):882-7 10878385 - J Immunol. 2000 Jul 15;165(2):1066-73 19368894 - Structure. 2009 Apr 15;17(4):611-9 17989688 - Nat Biotechnol. 2007 Nov;25(11):1256-64 18536718 - Nat Immunol. 2008 Jul;9(7):753-60 2025413 - Acta Crystallogr A. 1991 Mar 1;47 ( Pt 2):110-9 11287977 - N Engl J Med. 2001 Apr 5;344(14):1058-66 15728504 - J Immunol. 2005 Mar 1;174(5):2926-33 19503103 - Nat Immunol. 2009 Jul;10(7):721-7 12393927 - Acta Crystallogr D Biol Crystallogr. 2002 Nov;58(Pt 11):1948-54 17681537 - J Mol Biol. 2007 Sep 21;372(3):774-97 20133685 - Proc Natl Acad Sci U S A. 2010 Feb 23;107(8):3681-6 6586103 - Ann N Y Acad Sci. 1983;421:291-8 17848512 - Proc Natl Acad Sci U S A. 2007 Sep 18;104(38):15051-6 16683746 - Chem Rev. 2006 May;106(5):1589-615 16831446 - J Mol Biol. 2006 Aug 4;361(1):115-27 1740458 - J Biol Chem. 1992 Feb 25;267(6):4171-6 20417224 - Toxicon. 2010 Dec 15;56(7):1198-222 16177781 - Nature. 2005 Sep 22;437(7058):505-11 9489922 - Proteins. 1998 Feb 1;30(2):144-54 6912277 - J Exp Med. 1981 Sep 1;154(3):856-67 20545943 - Cell Microbiol. 2010 Oct;12(10):1506-16 3183384 - J Immunol. 1988 Dec 1;141(11):3895-901 19025125 - Adv Exp Med Biol. 2008;632:221-36 19503104 - Nat Immunol. 2009 Jul;10(7):728-33 20852386 - J Clin Invest. 2010 Oct;120(10):3702-12 19574954 - EMBO J. 2009 Aug 19;28(16):2469-78 10352274 - J Immunol. 1999 Jun 1;162(11):6580-8 17051150 - Nature. 2006 Nov 9;444(7116):217-20 7876551 - J Immunol. 1995 Mar 15;154(6):2808-20 19196712 - J Biol Chem. 2009 Apr 17;284(16):10473-9 10640753 - J Immunol. 2000 Feb 1;164(3):1379-85 15215472 - Nucleic Acids Res. 2004 Jul 1;32(Web Server issue):W665-7 11517324 - Proc Natl Acad Sci U S A. 2001 Aug 28;98(18):10037-41 9041627 - Protein Sci. 1997 Feb;6(2):263-74 20124699 - Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):190-7 17051160 - Nature. 2006 Nov 9;444(7116):213-6 18204047 - J Biol Chem. 2008 Mar 21;283(12):7853-63 12440962 - Biochem Soc Trans. 2002 Nov;30(Pt 6):1006-10 3495629 - J Exp Med. 1987 Jun 1;165(6):1494-507 17684013 - J Biol Chem. 2007 Oct 5;282(40):29241-7 15476920 - Mol Immunol. 2004 Nov;41(11):1089-98 |
References_xml | – volume: 41 start-page: 1089 year: 2004 end-page: 1098 ident: b12 publication-title: Mol Immunol contributor: fullname: Gasque, P – volume: 164 start-page: 1379 year: 2000 end-page: 1385 ident: b38 publication-title: J Immunol contributor: fullname: Pangburn, MK – volume: 66 start-page: 190 year: 2010 end-page: 197 ident: b5 publication-title: Acta Crystallogr D Biol Crystallogr contributor: fullname: Ealick, SE – volume: 98 start-page: 10037 year: 2001 end-page: 10041 ident: b3 publication-title: Proc Natl Acad Sci USA contributor: fullname: McCammon, JA – volume: 10 start-page: 728 year: 2009 end-page: 733 ident: b40 publication-title: Nat Immunol contributor: fullname: Gros, P – volume: 267 start-page: 4171 year: 1992 end-page: 4176 ident: b23 publication-title: J Biol Chem contributor: fullname: Kinoshita, T – volume: 444 start-page: 213 year: 2006 end-page: 216 ident: b16 publication-title: Nature contributor: fullname: Gros, P – year: 2001 ident: b21 publication-title: International Tables for Crystallography, Crystallography of Biological Macromolecules contributor: fullname: Kabsch, W – volume: 344 start-page: 1058 year: 2001 end-page: 1066 ident: b47 publication-title: N Engl J Med contributor: fullname: Walport, MJ – volume: 32 start-page: W665 year: 2004 end-page: W667 ident: b8 publication-title: Nucleic Acids Res contributor: fullname: Baker, NA – volume: 47 start-page: 2289 year: 2010 end-page: 2289 ident: b43 publication-title: Mol Immunol contributor: fullname: Lambris, JD – volume: 107 start-page: 3681 year: 2010 end-page: 3686 ident: b30 publication-title: Proc Natl Acad Sci USA contributor: fullname: Andersen, GR – volume: 56 start-page: 1198 year: 2010 end-page: 1222 ident: b46 publication-title: Toxicon contributor: fullname: Fritzinger, DC – volume: 30 start-page: 1006 year: 2002 end-page: 1010 ident: b35 publication-title: Biochem Soc Trans contributor: fullname: Rawal, N – volume: 31 start-page: 34 year: 1994 end-page: 38 ident: b6 publication-title: Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography contributor: fullname: Cowtan, K – volume: 9 start-page: 753 year: 2008 end-page: 760 ident: b11 publication-title: Nat Immunol contributor: fullname: Andersen, GR – volume: 437 start-page: 505 year: 2005 end-page: 511 ident: b19 publication-title: Nature contributor: fullname: Gros, P – volume: 284 start-page: 10473 year: 2009 end-page: 10479 ident: b22 publication-title: J Biol Chem contributor: fullname: Wiesmann, C – volume: 47 start-page: 2257 year: 2010 end-page: 2258 ident: b14 publication-title: Mol Immunol contributor: fullname: Gros, P – volume: 30 start-page: 144 year: 1998 end-page: 154 ident: b15 publication-title: Proteins contributor: fullname: Berendsen, HJ – volume: 10 start-page: 728 year: 2009 end-page: 733 ident: b49 publication-title: Nat Immunol contributor: fullname: Gros, P – volume: 17 start-page: 611 year: 2009 end-page: 619 ident: b26 publication-title: Structure contributor: fullname: Narayana, SV – volume: 106 start-page: 882 year: 2009 end-page: 887 ident: b45 publication-title: Proc Natl Acad Sci USA contributor: fullname: Llorca, O – volume: 421 start-page: 291 year: 1983 end-page: 298 ident: b34 publication-title: Ann NY Acad Sci contributor: fullname: Muller-Eberhard, HJ – volume: 361 start-page: 115 year: 2006 end-page: 127 ident: b10 publication-title: J Mol Biol contributor: fullname: Sottrup-Jensen, L – volume: 283 start-page: 7853 year: 2008 end-page: 7863 ident: b39 publication-title: J Biol Chem contributor: fullname: Salvi, VP – volume: 12 start-page: 1506 year: 2010 end-page: 1516 ident: b4 publication-title: Cell Microbiol contributor: fullname: de Haas, CJ – volume: 154 start-page: 2808 year: 1995 end-page: 2820 ident: b9 publication-title: J Immunol contributor: fullname: Isenman, DE – volume: 165 start-page: 1494 year: 1987 end-page: 1507 ident: b44 publication-title: J Exp Med contributor: fullname: Inoue, K – volume: 25 start-page: 1256 year: 2007 end-page: 1264 ident: b41 publication-title: Nat Biotechnol contributor: fullname: Bell, L – year: 2002 ident: b7 publication-title: The PyMOL User's Manual contributor: fullname: DeLano, WL – volume: 162 start-page: 6580 year: 1999 end-page: 6588 ident: b32 publication-title: J Immunol contributor: fullname: Ogata, RT – volume: 165 start-page: 1066 year: 2000 end-page: 1073 ident: b42 publication-title: J Immunol contributor: fullname: Ogata, RT – volume: 444 start-page: 217 year: 2006 end-page: 220 ident: b48 publication-title: Nature contributor: fullname: van Lookeren Campagne, M – volume: 632 start-page: 221 year: 2008 end-page: 236 ident: b13 publication-title: Adv Exp Med Biol contributor: fullname: Geisbrecht, BV – volume: 154 start-page: 856 year: 1981 end-page: 867 ident: b36 publication-title: J Exp Med contributor: fullname: Muller-Eberhard, HJ – volume: 47 start-page: 110 year: 1991 end-page: 119 ident: b20 publication-title: Acta Cryst A contributor: fullname: Kjeldgaard, M – volume: 372 start-page: 774 year: 2007 end-page: 797 ident: b27 publication-title: J Mol Biol contributor: fullname: Henrick, K – volume: 26 start-page: 283 year: 1993 end-page: 291 ident: b29 publication-title: J Appl Cryst contributor: fullname: Thornton, JM – volume: 120 start-page: 3702 year: 2010 end-page: 3712 ident: b33 publication-title: J Clin Invest contributor: fullname: Rodriguez de Cordoba, S – volume: 282 start-page: 29241 year: 2007 end-page: 29247 ident: b18 publication-title: J Biol Chem contributor: fullname: Gros, P – volume: 6 start-page: 263 year: 1997 end-page: 274 ident: b31 publication-title: Protein Sci contributor: fullname: Dodds, AW – volume: 174 start-page: 2926 year: 2005 end-page: 2933 ident: b28 publication-title: J Immunol contributor: fullname: Fraser, JD – start-page: 59 year: 1994 end-page: 66 ident: b25 publication-title: From First Map to Final Model contributor: fullname: Jones, TA – volume: 104 start-page: 15051 year: 2007 end-page: 15056 ident: b37 publication-title: Proc Natl Acad Sci USA contributor: fullname: Wines, BD – volume: 28 start-page: 2469 year: 2009 end-page: 2478 ident: b17 publication-title: EMBO J contributor: fullname: Gros, P – volume: 106 start-page: 1589 year: 2006 end-page: 1615 ident: b2 publication-title: Chem Rev contributor: fullname: McCammon, JA – volume: 58 start-page: 1948 year: 2002 end-page: 1954 ident: b1 publication-title: Acta Crystallogr D Biol Crystallogr contributor: fullname: Terwilliger, TC – volume: 141 start-page: 3895 year: 1988 end-page: 3901 ident: b24 publication-title: J Immunol contributor: fullname: Inoue, K – volume: 47 start-page: 110 year: 1991 end-page: 119 article-title: Improved methods for building protein models in electron density maps and the location of errors in these models publication-title: Acta Cryst A – volume: 437 start-page: 505 year: 2005 end-page: 511 article-title: Structures of complement component C3 provide insights into the function and evolution of immunity publication-title: Nature – volume: 98 start-page: 10037 year: 2001 end-page: 10041 article-title: Electrostatics of nanosystems: application to microtubules and the ribosome publication-title: Proc Natl Acad Sci USA – volume: 9 start-page: 753 year: 2008 end-page: 760 article-title: Structure of and influence of a tick complement inhibitor on human complement component 5 publication-title: Nat Immunol – volume: 47 start-page: 2257 year: 2010 end-page: 2258 article-title: Structural insights into the initiation of the terminal pathway publication-title: Mol Immunol – volume: 283 start-page: 7853 year: 2008 end-page: 7863 article-title: Activation of complement component C5: comparison of C5 convertases of the lectin pathway and the classical pathway of complement publication-title: J Biol Chem – volume: 106 start-page: 1589 year: 2006 end-page: 1615 article-title: Molecular dynamics: survey of methods for simulating the activity of proteins publication-title: Chem Rev – volume: 25 start-page: 1256 year: 2007 end-page: 1264 article-title: Discovery and development of the complement inhibitor eculizumab for the treatment of paroxysmal nocturnal hemoglobinuria publication-title: Nat Biotechnol – volume: 30 start-page: 1006 year: 2002 end-page: 1010 article-title: Structure and function of complement C5 convertase enzymes publication-title: Biochem Soc Trans – volume: 141 start-page: 3895 year: 1988 end-page: 3901 article-title: C5 convertase of the alternative complement pathway: covalent linkage between two C3b molecules within the trimolecular complex enzyme publication-title: J Immunol – volume: 421 start-page: 291 year: 1983 end-page: 298 article-title: Initiation of the alternative complement pathway due to spontaneous hydrolysis of the thioester of C3 publication-title: Ann NY Acad Sci – volume: 372 start-page: 774 year: 2007 end-page: 797 article-title: Inference of macromolecular assemblies from crystalline state publication-title: J Mol Biol – volume: 10 start-page: 728 year: 2009 end-page: 733 article-title: Structural and functional implications of the alternative complement pathway C3 convertase stabilized by a staphylococcal inhibitor publication-title: Nat Immunol – volume: 106 start-page: 882 year: 2009 end-page: 887 article-title: 3D structure of the C3bB complex provides insights into the activation and regulation of the complement alternative pathway convertase publication-title: Proc Natl Acad Sci USA – year: 2001 article-title: XDS publication-title: International Tables for Crystallography, Crystallography of Biological Macromolecules – year: 2002 publication-title: The PyMOL User's Manual – volume: 10 start-page: 728 year: 2009 end-page: 733 article-title: Structure of complement fragment C3b‐factor H and implications for host protection by complement regulators publication-title: Nat Immunol – volume: 361 start-page: 115 year: 2006 end-page: 127 article-title: The structure of bovine complement component 3 reveals the basis for thioester function publication-title: J Mol Biol – volume: 165 start-page: 1494 year: 1987 end-page: 1507 article-title: Covalent association of C3b with C4b within C5 convertase of the classical complement pathway publication-title: J Exp Med – volume: 164 start-page: 1379 year: 2000 end-page: 1385 article-title: Functional role of the noncatalytic subunit of complement C5 convertase publication-title: J Immunol – volume: 120 start-page: 3702 year: 2010 end-page: 3712 article-title: Human C3 mutation reveals a mechanism of dense deposit disease pathogenesis and provides insights into complement activation and regulation publication-title: J Clin Invest – volume: 47 start-page: 2289 year: 2010 end-page: 2289 article-title: Impaired ability of complement activation via the alternative pathway C3 convertase caused by a single‐point mutation in the beta chain of C3 publication-title: Mol Immunol – volume: 31 start-page: 34 year: 1994 end-page: 38 article-title: ‘Dm’: an automated procedure for phase improvement by density modification publication-title: Joint CCP4 and ESF‐EACBM Newsletter on Protein Crystallography – volume: 344 start-page: 1058 year: 2001 end-page: 1066 article-title: Complement. First of two parts publication-title: N Engl J Med – volume: 41 start-page: 1089 year: 2004 end-page: 1098 article-title: Complement: a unique innate immune sensor for danger signals publication-title: Mol Immunol – volume: 282 start-page: 29241 year: 2007 end-page: 29247 article-title: Structure of compstatin in complex with complement component C3c reveals a new mechanism of complement inhibition publication-title: J Biol Chem – volume: 17 start-page: 611 year: 2009 end-page: 619 article-title: The crystal structure of cobra venom factor, a cofactor for C3‐ and C5‐convertase CVFBb publication-title: Structure – volume: 267 start-page: 4171 year: 1992 end-page: 4176 article-title: Covalent binding of C3b to C4b within the classical complement pathway C5 convertase. Determination of amino acid residues involved in ester linkage formation publication-title: J Biol Chem – volume: 30 start-page: 144 year: 1998 end-page: 154 article-title: Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme publication-title: Proteins – volume: 284 start-page: 10473 year: 2009 end-page: 10479 article-title: Structural and functional analysis of a C3b‐specific antibody that selectively inhibits the alternative pathway of complement publication-title: J Biol Chem – volume: 107 start-page: 3681 year: 2010 end-page: 3686 article-title: Structural basis for inhibition of complement C5 by the SSL7 protein from Staphylococcus aureus publication-title: Proc Natl Acad Sci USA – volume: 66 start-page: 190 year: 2010 end-page: 197 article-title: Structure of human desArg‐C5a publication-title: Acta Crystallogr D Biol Crystallogr – volume: 12 start-page: 1506 year: 2010 end-page: 1516 article-title: Functional basis for complement evasion by staphylococcal superantigen‐like 7 publication-title: Cell Microbiol – volume: 165 start-page: 1066 year: 2000 end-page: 1073 article-title: Distal recognition site for classical pathway convertase located in the C345C/netrin module of complement component C5 publication-title: J Immunol – volume: 162 start-page: 6580 year: 1999 end-page: 6588 article-title: Active sites in complement components C5 and C3 identified by proximity to indels in the C3/4/5 protein family publication-title: J Immunol – volume: 28 start-page: 2469 year: 2009 end-page: 2478 article-title: Insights into complement convertase formation based on the structure of the factor B‐cobra venom factor complex publication-title: EMBO J – volume: 58 start-page: 1948 year: 2002 end-page: 1954 article-title: PHENIX: building new software for automated crystallographic structure determination publication-title: Acta Crystallogr D Biol Crystallogr – volume: 632 start-page: 221 year: 2008 end-page: 236 article-title: Staphylococcal complement inhibitors: biological functions, recognition of complement components, and potential therapeutic implications publication-title: Adv Exp Med Biol – volume: 444 start-page: 213 year: 2006 end-page: 216 article-title: Structure of C3b reveals conformational changes that underlie complement activity publication-title: Nature – volume: 154 start-page: 2808 year: 1995 end-page: 2820 article-title: Evidence for the involvement of arginine 462 and the flanking sequence of human C4 beta‐chain in mediating C5 binding to the C4b subcomponent of the classical complement pathway C5 convertase publication-title: J Immunol – volume: 56 start-page: 1198 year: 2010 end-page: 1222 article-title: Cobra venom factor: structure, function, and humanization for therapeutic complement depletion publication-title: Toxicon – volume: 154 start-page: 856 year: 1981 end-page: 867 article-title: Formation of the initial C3 convertase of the alternative complement pathway. Acquisition of C3b‐like activities by spontaneous hydrolysis of the putative thioester in native C3 publication-title: J Exp Med – volume: 32 start-page: W665 year: 2004 end-page: W667 article-title: PDB2PQR: an automated pipeline for the setup of Poisson‐Boltzmann electrostatics calculations publication-title: Nucleic Acids Res – volume: 26 start-page: 283 year: 1993 end-page: 291 article-title: PROCHECK: a program to check the stereochemical quality of protein structures publication-title: J Appl Cryst – volume: 444 start-page: 217 year: 2006 end-page: 220 article-title: Structure of C3b in complex with CRIg gives insights into regulation of complement activation publication-title: Nature – volume: 174 start-page: 2926 year: 2005 end-page: 2933 article-title: The staphylococcal superantigen‐like protein 7 binds IgA and complement C5 and inhibits IgA‐Fc alpha RI binding and serum killing of bacteria publication-title: J Immunol – start-page: 59 year: 1994 end-page: 66 article-title: Halloween… masks and bones publication-title: From First Map to Final Model – volume: 6 start-page: 263 year: 1997 end-page: 274 article-title: The internal thioester and the covalent binding properties of the complement proteins C3 and C4 publication-title: Protein Sci – volume: 104 start-page: 15051 year: 2007 end-page: 15056 article-title: Structural basis for evasion of IgA immunity by Staphylococcus aureus revealed in the complex of SSL7 with Fc of human IgA1 publication-title: Proc Natl Acad Sci USA |
SSID | ssj0005871 |
Score | 2.3334644 |
Snippet | Complement acts as a danger‐sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the... Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the... Activation of the complement system by proteolytic cleavage leads to an inflammatory response. The complement components C3 and C5 are cleaved by convertases.... |
SourceID | pubmedcentral proquest pubmed wiley nature istex |
SourceType | Open Access Repository Aggregation Database Index Database Publisher |
StartPage | 606 |
SubjectTerms | Complement C3-C5 Convertases - chemistry Complement C3-C5 Convertases - metabolism Complement C5 - chemistry Complement C5 - metabolism complement system Crystallography Elapid Venoms - chemistry Elapid Venoms - metabolism Exotoxins - chemistry Exotoxins - metabolism Humans immunology Models, Molecular Molecular biology Multiprotein Complexes - chemistry Multiprotein Complexes - metabolism Proteases protein complex Protein Conformation Proteins proteolytic regulation structural biology Substrates |
SummonAdditionalLinks | – databaseName: Health & Medical Collection dbid: 7X7 link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Lb9QwELZKK0QvCMqjSwH5gLhF6zgv-4To9qWi7omKvSDLT1FQk9LdSu2_Z8ZOQpdKSLnZSRyPM_PN-PMMIR8q60tZapvVgbGsNFZn2uMB5soaW-dgYgOedz6b1yfn5emiWmyQ4-EsDNIqB50YFbXrLMbIpwKQNSZPKafaYBDArqafrn5nWD4Kt1n7WhqPyFbOAVXAwm4WzV-uh4ieVwy2lLmQQ_bGQkz9pel-JopXgWXht3B2b_9NrLkGPB_yJ-_j2miYjp6Rpz2ipJ_TEnhONny7Qx6nGpN3O-TJbCjp9oJ8RzUR09HSkTjUtdTc0cgsj5FCGnnogMmXfkkxvxNYEEcvWgpIkc6qzHbgX1NQkd0lTcV6-ptvX5Lzo8Ovs5Osr6-QWSyKmWnQc2XOtXVM12CmPKANIZ0LQQdeWRaYlTlH0lWoRMFcqGUuG8udEKHU4Ny-Iptt1_pdQq0B6Mdd7WUBgmLGOBukYbX3jXOGuQn5GOdVXaUcGkpf_0JKWVOpb_NjxWfyYM7zL4pPyF6a-LFnFBDKB8QDrYM0VP-vLdW4MiaEjq0wsbjzoVvf3WAXidhSwANeJ9GNjwfTnTfghE1IsybUsQPm315vaS9-xDzcYP3BO4XXsij-8Y64r1-INHKFQ1cwdnV4tn_af8eb_37HHtlOkWsO11uyubq-8e8A-qzM-7is_wCUDQLO priority: 102 providerName: ProQuest |
Title | Substrate recognition by complement convertases revealed in the C5-cobra venom factor complex |
URI | https://api.istex.fr/ark:/67375/WNG-2C9DN21K-2/fulltext.pdf http://dx.doi.org/10.1038/emboj.2010.341 https://onlinelibrary.wiley.com/doi/abs/10.1038%2Femboj.2010.341 https://www.ncbi.nlm.nih.gov/pubmed/21217642 https://www.proquest.com/docview/848700364/abstract/ https://search.proquest.com/docview/849008581 https://pubmed.ncbi.nlm.nih.gov/PMC3034014 |
Volume | 30 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1bb9MwFD7aRQheEIxbGVR-QLxldRIncR5Z1jE2tZoQE32zfBUFmkzrJm1v_Af-Ib-EY-ciCm9IVaXKTuL62MffcT5_B-BNpi0rmdRR7iiNmNIyktYfYM600nmMS6zz551n8_zkgp0ussUWZP1ZmEDa12p5UH9fHdTLL4FbebnSk54nNjmfVeh2MSxgk23YLtK0D9F7XgcPUVbYWGExL3ulxpRP7Eo1X1s6FzrvoAOMiDz3adp3fafe_q2nuYE3_6VN_glnw3p0_AgedkCSvGsb_Bi2bL0H99rUknd7cL_qM7k9AeG9Q1ChJQNfqKmJuiOBUB42CEmgnyMUX9s18bJOuHAYsqwJAkRSZb9-_NQNBtYEfWOzIm2Wnu7y26dwcTz9VJ1EXWKFSPtsmJFEB8fiRGpDZY7rk0WYwUtjnJMuyTR1VJdx4tlWLuMpNS4v47LQieHcMYlR7TPYqZvavgCiFWK-xOS2TDnjVCmjXalobm1hjKJmBG9Dz4rLVjxDyKtvnktWZOLz_L1IqvJonsRnIhnBftv1Q81gLW8stBWW9vYQ3SRbC3xg4fV02AjIUIpd6195yNo2N75K6UElxxs8b4033L63_QiKDbMOFbzw9mYJjscgwN2NvxHQMACGK8IL_ZS3LRe-6QLbLqazw9Puf7z874ftw4N2OzvBzyvYub66sa8RD12rMc6CRYHfvIrHsHs4nZ9_xF9HH87GYWb8BomwDls |
link.rule.ids | 230,315,733,786,790,891,12083,12250,21416,27957,27958,31754,31755,33301,33302,33779,33780,43345,43614,43840,53827,53829 |
linkProvider | National Library of Medicine |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Lb9QwELZgV6i9ICivpTx8QNyiOs7LPiG6bFnaboRQK3pBlp-iVE1Kt5Xaf8-Mkw0sSEi52UmcGWfmG_vzDCFvCutzmWublIGxJDdWJ9rjAebCGlum4GIDnnde1OX8ON8_KU56bs6yp1WubGI01K61uEa-IwBZY_KU_N3FzwSLRuHmal9B4y4Z5xlEKiMy3p3Vn7_85niIGHHFRZY8FXKVtTETO_7ctD86aleG5eDHKNWbvxNqrgHOf3mTf-LZ6JD2HpD7PZKk7zvVPyR3fLNF7nW1JW-3yMZ0VcrtEfmG5iGmoaUDYahtqLmlkVEeVwhp5J8DFl_6JcW8TuA5HD1tKCBEOi0S20JcTcE0tue0K9LT33zzmBzvzY6m86Svq5BYLIaZaLBvecq1dUyX4J48oAwhnQtBB15YFpiVKUeyVShExlwoZSory50QIdcQ1D4ho6Zt_DNCrQHIx13pJchfMGOcDdKw0vvKOcPchLyNclUXXe4MpS_PkEpWFepr_VHxqfxQ8_RA8QnZ7gQ_9IwKQv2AeqB1pQ3V_2NLNcyICaFDKwgWdzx049tr7CIRUwp4wNNOdcPjwWWnFQRfE1KtKXXogHm311ua0-8x_zZ4fYhK4bUsqn-4I-7nZ6IbucKhKxi7mi129_vveP7f73hNNuZHi0N1-Kk-2Cab3eo1h-sFGV1dXvuXAH-uzKt-kv8Cz00DZw |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3LbtQwFLWgFY8Nj1JKKA8vELtMHuMk9hLSDqVlRl1QUbGx4pcY2klGnRmpZcU_8Id8Cdd2EnXKrlJ2dhI_rq_PdU7ORehdJjVhpJJhbuI4JEJWYaXtD8yZFDJPYIs19n_n8SQ_OCGHp9nptVRfjrQvxXRQn88G9fSH41bOZzLqeGLR8bgEtwthAYnmykR30Sas2ZR1gXrH7qAu1nLHKyShrNNrHNJIz0Tz05O6wIU7NWDA5blN1r5ph_bypqrmGur8nzx5HdS6XWn0GH3v-uPJKGeD1VIM5K8bUo-36vAT9KjFqviDr_IU3dH1Frrns1debaEHZZcs7hni1gE5oVvcU5KaGosr7Djr7gwSO4Y7oP2FXmCrHAV7k8LTGgMGxWX29_cf2UDsjsH9NjPsEwG1t19uo5PR_tfyIGxzN4TSJtwMK_ChJEkrqeIqhy1QA5KhTCljKpNmMjaxZElqCV0mo8NYmZwlrJCpotSQCgLn52ijbmr9AmEpAFamKtdsSAmNhVDSMBHnWhdKiVgF6L2bNj73-hy8ujizdLUi498mn3hasr1JmhzxNEC7fl77ms4UrCWAIUBpN9m8XccLDi8srGQPCRDuS2Fo7VeVqtbNylZhFrdSeMCOt4z-8Z1hBahYs5m-gtX2Xi8BC3Aa3-2MByh21tXf4TgDQ-pbzm3TObSd748_Hrb9eHnrl71F94_3RvzL58nRLnroD89TuF6hjeXFSr8G9LUUb9w6-wffEC57 |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Substrate+recognition+by+complement+convertases+revealed+in+the+C5-cobra+venom+factor+complex&rft.jtitle=The+EMBO+journal&rft.au=Andersen%2C+Gregers+R&rft.au=Laursen%2C+Nick+S&rft.au=Andersen%2C+Kasper+R&rft.au=Braren%2C+Ingke&rft.date=2011-02-02&rft.issn=0261-4189&rft.eissn=1460-2075&rft.volume=30&rft.issue=3&rft.spage=606&rft.epage=616&rft_id=info:doi/10.1038%2Femboj.2010.341&rft.externalDocID=emboj2010341 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0261-4189&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0261-4189&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0261-4189&client=summon |