Domain 2 of Nonstructural Protein 5A (NS5A) of Hepatitis C Virus Is Natively Unfolded
Nonstructural protein 5A protein (NS5A) of hepatitis C virus (HCV) plays an important role in the regulation of viral replication, interferon resistance, and apoptosis. HCV NS5A comprises three domains. Recently the structure of domain 1 has been determined, revealing a structural scaffold with a no...
Saved in:
Published in | Biochemistry (Easton) Vol. 46; no. 41; pp. 11550 - 11558 |
---|---|
Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
United States
American Chemical Society
16.10.2007
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Nonstructural protein 5A protein (NS5A) of hepatitis C virus (HCV) plays an important role in the regulation of viral replication, interferon resistance, and apoptosis. HCV NS5A comprises three domains. Recently the structure of domain 1 has been determined, revealing a structural scaffold with a novel zinc-binding motif and a disulfide bond. At present, the structures of domains 2 and 3 remain undefined. Domain 2 of HCV NS5A (NS5A-D2) is important for functions of NS5A and involved in molecular interactions with its own NS5B and PKR, a cellular interferon-inducible serine/threonine specific protein kinase. In this study we performed structural analysis of domain 2 by multinuclear nuclear magnetic resonance (NMR) spectroscopy. The analysis of the backbone 1H, 13C, and 15N resonances, 3 J HN α coupling constants ,and 3D NOE data indicates that NS5A-D2 lacks secondary structural elements and reveals characteristics of unfolded proteins. NMR relaxation parameters confirmed the lack of rigid structure in the domain. The absence of an ordered conformation and the observation of a highly dynamic behavior of NS5A-D2 may provide an underlying molecular basis on its physiological function to allow NS5A-D2 to interact with a variety of biological partners. |
---|---|
AbstractList | Nonstructural protein 5A protein (NS5A) of hepatitis C virus (HCV) plays an important role in the regulation of viral replication, interferon resistance, and apoptosis. HCV NS5A comprises three domains. Recently the structure of domain 1 has been determined, revealing a structural scaffold with a novel zinc-binding motif and a disulfide bond. At present, the structures of domains 2 and 3 remain undefined. Domain 2 of HCV NS5A (NS5A-D2) is important for functions of NS5A and involved in molecular interactions with its own NS5B and PKR, a cellular interferon-inducible serine/threonine specific protein kinase. In this study we performed structural analysis of domain 2 by multinuclear nuclear magnetic resonance (NMR) spectroscopy. The analysis of the backbone super(1)H, super(13)C, and super(15)N resonances, super(3)J sub(HN alpha ) coupling constants, and 3D NOE data indicates that NS5A-D2 lacks secondary structural elements and reveals characteristics of unfolded proteins. NMR relaxation parameters confirmed the lack of rigid structure in the domain. The absence of an ordered conformation and the observation of a highly dynamic behavior of NS5A-D2 may provide an underlying molecular basis on its physiological function to allow NS5A-D2 to interact with a variety of biological partners. Nonstructural protein 5A protein (NS5A) of hepatitis C virus (HCV) plays an important role in the regulation of viral replication, interferon resistance, and apoptosis. HCV NS5A comprises three domains. Recently the structure of domain 1 has been determined, revealing a structural scaffold with a novel zinc-binding motif and a disulfide bond. At present, the structures of domains 2 and 3 remain undefined. Domain 2 of HCV NS5A (NS5A-D2) is important for functions of NS5A and involved in molecular interactions with its own NS5B and PKR, a cellular interferon-inducible serine/threonine specific protein kinase. In this study we performed structural analysis of domain 2 by multinuclear nuclear magnetic resonance (NMR) spectroscopy. The analysis of the backbone 1H, 13C, and 15N resonances, 3 J HN α coupling constants ,and 3D NOE data indicates that NS5A-D2 lacks secondary structural elements and reveals characteristics of unfolded proteins. NMR relaxation parameters confirmed the lack of rigid structure in the domain. The absence of an ordered conformation and the observation of a highly dynamic behavior of NS5A-D2 may provide an underlying molecular basis on its physiological function to allow NS5A-D2 to interact with a variety of biological partners. Nonstructural protein 5A protein (NS5A) of hepatitis C virus (HCV) plays an important role in the regulation of viral replication, interferon resistance, and apoptosis. HCV NS5A comprises three domains. Recently the structure of domain 1 has been determined, revealing a structural scaffold with a novel zinc-binding motif and a disulfide bond. At present, the structures of domains 2 and 3 remain undefined. Domain 2 of HCV NS5A (NS5A-D2) is important for functions of NS5A and involved in molecular interactions with its own NS5B and PKR, a cellular interferon-inducible serine/threonine specific protein kinase. In this study we performed structural analysis of domain 2 by multinuclear nuclear magnetic resonance (NMR) spectroscopy. The analysis of the backbone 1H, 13C, and 15N resonances, 3JHNalpha coupling constants ,and 3D NOE data indicates that NS5A-D2 lacks secondary structural elements and reveals characteristics of unfolded proteins. NMR relaxation parameters confirmed the lack of rigid structure in the domain. The absence of an ordered conformation and the observation of a highly dynamic behavior of NS5A-D2 may provide an underlying molecular basis on its physiological function to allow NS5A-D2 to interact with a variety of biological partners. |
Author | Liang, Yu Kang, Cong Bao Ye, Hong Yoon, Ho Sup |
Author_xml | – sequence: 1 givenname: Yu surname: Liang fullname: Liang, Yu – sequence: 2 givenname: Hong surname: Ye fullname: Ye, Hong – sequence: 3 givenname: Cong Bao surname: Kang fullname: Kang, Cong Bao – sequence: 4 givenname: Ho Sup surname: Yoon fullname: Yoon, Ho Sup |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/17880107$$D View this record in MEDLINE/PubMed |
BookMark | eNqF0MtqGzEUBmAREhLnsugLFG1a6sWkRzO6zdK4FwcSN-DLVsijMzDpeORIM6V5-8rYpJtAVkI6H78O_yU57XyHhHxgcMsgZ183jQJQSuIJGTGRQ8bLUpySEQDILC8lXJDLGJ_SlYPi5-SCKa2BgRqR1Te_tU1Hc-prOvdd7MNQ9UOwLX0Mvsc0EhP6Zb4Qk_GezHBn-6ZvIp3SdROGSO8inaenP9i-0FVX-9ahuyZntW0j3hzPK7L68X05nWX3v37eTSf3meVc95l03DpbO-FAgQDOlJA5Z6K0DqqirHWe9tUbyaSssLQatXACC7URheYOeXFFPh9yd8E_Dxh7s21ihW1rO_RDNFIXkuUg3oXJSKZgnzg-wCr4GAPWZhearQ0vhoHZl21ey0724zF02GzR_ZfHdhPIDqCJPf59ndvw20hVKGGWjwujH_J1-bBmRib_6eBtFc2TH0KXynvj438T9pNF |
CitedBy_id | crossref_primary_10_1155_2016_8341937 crossref_primary_10_1155_2014_467452 crossref_primary_10_1016_j_bbrc_2009_02_108 crossref_primary_10_1021_ac902550n crossref_primary_10_1016_j_bbrc_2014_04_053 crossref_primary_10_1099_jgv_0_000009 crossref_primary_10_1128_JVI_00253_11 crossref_primary_10_1007_s12104_011_9309_2 crossref_primary_10_1021_jm401793m crossref_primary_10_1128_JVI_06641_11 crossref_primary_10_1074_jbc_M117_813766 crossref_primary_10_1128_JVI_01582_14 crossref_primary_10_1007_s10858_012_9618_5 crossref_primary_10_1074_jbc_RA119_009537 crossref_primary_10_3390_pathogens11010102 crossref_primary_10_1074_jbc_M809244200 crossref_primary_10_1128_AAC_00808_16 crossref_primary_10_1128_JVI_00616_10 crossref_primary_10_1074_jbc_M110_182436 crossref_primary_10_1074_jbc_M115_644419 crossref_primary_10_1128_JVI_03017_13 crossref_primary_10_1128_JVI_02352_08 crossref_primary_10_1021_acs_biochem_7b00212 crossref_primary_10_1128_JVI_01677_14 crossref_primary_10_1128_AAC_00556_10 crossref_primary_10_1128_JVI_02995_14 crossref_primary_10_1128_JVI_02861_12 crossref_primary_10_1517_14656566_2014_972364 crossref_primary_10_1128_JVI_00215_11 crossref_primary_10_1039_D0CP06360F crossref_primary_10_1186_1472_6807_12_28 crossref_primary_10_1186_1743_422X_9_14 crossref_primary_10_1371_journal_pone_0013687 crossref_primary_10_1128_JVI_00393_11 crossref_primary_10_1016_j_jmb_2012_04_023 crossref_primary_10_1016_j_jmb_2007_11_055 crossref_primary_10_1016_j_coviro_2014_04_012 crossref_primary_10_1080_02648725_2018_1467151 crossref_primary_10_1039_C4MB00027G crossref_primary_10_1038_srep04765 crossref_primary_10_1002_pro_2456 crossref_primary_10_3390_v4112598 crossref_primary_10_1074_jbc_M112_392209 crossref_primary_10_1099_jgv_0_001000 crossref_primary_10_1021_cr4005692 crossref_primary_10_1042_BSR20090035 crossref_primary_10_1371_journal_ppat_1005376 crossref_primary_10_1371_journal_pone_0039261 crossref_primary_10_3390_ph14040292 crossref_primary_10_1016_j_coviro_2013_06_014 crossref_primary_10_1016_j_ddtec_2011_11_002 crossref_primary_10_1038_srep26401 crossref_primary_10_3390_v5071684 crossref_primary_10_1016_j_virusres_2012_09_007 crossref_primary_10_1016_j_coviro_2013_03_013 crossref_primary_10_1371_journal_ppat_1001118 crossref_primary_10_4049_jimmunol_1201497 crossref_primary_10_1016_j_bbamem_2011_05_014 crossref_primary_10_1371_journal_ppat_1002576 crossref_primary_10_1099_vir_0_050633_0 crossref_primary_10_1186_1743_422X_10_251 crossref_primary_10_1002_cbic_201500551 |
Cites_doi | 10.1002/ijc.11303 10.1074/jbc.M301615200 10.1074/jbc.M312245200 10.1126/science.274.5289.948 10.1006/jmbi.1994.0015 10.1023/A:1008393903034 10.1016/S0959-440X(02)00289-0 10.1016/S0168-8278(99)80392-4 10.1002/j.1460-2075.1996.tb00329.x 10.1128/JVI.79.8.5006-5016.2005 10.1046/j.0014-2956.2001.02649.x 10.1074/jbc.M111289200 10.1016/S0021-9258(18)45957-1 10.1021/ja00849a040 10.1002/hep.20032 10.1128/jvi.68.6.3753-3760.1994 10.1016/S0968-0004(03)00003-3 10.1128/jvi.71.11.8416-8428.1997 10.1074/jbc.C500423200 10.1074/jbc.M407787200 10.1006/bbrc.2001.4627 10.1016/j.jmb.2005.01.039 10.1016/0959-440X(92)90169-8 10.1006/jmbi.1999.3110 10.1023/A:1008307323283 10.1007/BF00175245 10.1007/BF00227466 10.1016/0022-2836(91)90214-Q 10.1007/BF00227471 10.1074/jbc.M111392200 10.1016/S1016-8478(23)17385-7 |
ContentType | Journal Article |
Copyright | Copyright © 2007 American Chemical Society |
Copyright_xml | – notice: Copyright © 2007 American Chemical Society |
DBID | BSCLL CGR CUY CVF ECM EIF NPM AAYXX CITATION 7U9 H94 7X8 |
DOI | 10.1021/bi700776e |
DatabaseName | Istex Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef Virology and AIDS Abstracts AIDS and Cancer Research Abstracts MEDLINE - Academic |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef AIDS and Cancer Research Abstracts Virology and AIDS Abstracts MEDLINE - Academic |
DatabaseTitleList | AIDS and Cancer Research Abstracts MEDLINE |
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 |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Anatomy & Physiology Chemistry |
EISSN | 1520-4995 |
EndPage | 11558 |
ExternalDocumentID | 10_1021_bi700776e 17880107 ark_67375_TPS_8M2V9MV1_6 a206903654 |
Genre | Research Support, Non-U.S. Gov't Journal Article |
GroupedDBID | - .K2 02 08R 23N 3O- 4.4 53G 55 55A 5GY 5RE 5VS 7~N 85S AABXI ABFLS ABMVS ABOCM ABPTK ABUCX ABUFD ACGFS ACJ ACNCT ACS AEESW AENEX AETEA AFEFF AFFNX AIDAL AJYGW ALMA_UNASSIGNED_HOLDINGS ANTXH AQSVZ BAANH CS3 D0L DU5 DZ EBS ED ED~ EJD F5P GNL IH9 IHE JG JG~ K2 K78 KM L7B LG6 OHT P2P ROL TN5 UI2 UNC UQL VF5 VG9 VQA W1F WH7 X X7M YZZ ZA5 --- -DZ -~X .55 6TJ ABJNI ABQRX ADHLV AGXLV AHGAQ BSCLL CUPRZ GGK XSW ZCA ~02 ~KM CGR CUY CVF ECM EIF NPM AAYXX ACRPL ADNMO CITATION 7U9 H94 7X8 |
ID | FETCH-LOGICAL-a448t-6d4adafd5d070504175624159ad0c39f824078b6166ce9a8e85d5e37b5384de43 |
IEDL.DBID | ACS |
ISSN | 0006-2960 |
IngestDate | Wed Dec 04 14:07:21 EST 2024 Fri Oct 25 04:36:00 EDT 2024 Fri Dec 06 02:49:00 EST 2024 Sat Sep 28 08:23:22 EDT 2024 Wed Oct 30 09:38:59 EDT 2024 Thu Aug 27 13:41:57 EDT 2020 |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 41 |
Language | English |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-a448t-6d4adafd5d070504175624159ad0c39f824078b6166ce9a8e85d5e37b5384de43 |
Notes | ark:/67375/TPS-8M2V9MV1-6 istex:91B2A4788A42142AF82F352F14BC5F9092E56ACD This study was partly supported by Singapore Cancer Syndicate Grant ZU44. ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
PMID | 17880107 |
PQID | 20561704 |
PQPubID | 23462 |
PageCount | 9 |
ParticipantIDs | proquest_miscellaneous_68361205 proquest_miscellaneous_20561704 crossref_primary_10_1021_bi700776e pubmed_primary_17880107 istex_primary_ark_67375_TPS_8M2V9MV1_6 acs_journals_10_1021_bi700776e |
ProviderPackageCode | JG~ 55A AABXI GNL VF5 7~N ACJ VG9 W1F ANTXH ACS AEESW AFEFF .K2 ABMVS ABUCX IH9 BAANH AQSVZ ED~ UI2 |
PublicationCentury | 2000 |
PublicationDate | 2007-10-16 |
PublicationDateYYYYMMDD | 2007-10-16 |
PublicationDate_xml | – month: 10 year: 2007 text: 2007-10-16 day: 16 |
PublicationDecade | 2000 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States |
PublicationTitle | Biochemistry (Easton) |
PublicationTitleAlternate | Biochemistry |
PublicationYear | 2007 |
Publisher | American Chemical Society |
Publisher_xml | – name: American Chemical Society |
References | Street A. (bi700776eb00018/bi700776eb00018_1) 2005; 79 Cleland J. L. (bi700776eb00060/bi700776eb00060_1) 1990 Johnson B. A. B. R. A. (bi700776eb00020/bi700776eb00020_1) 1994; 4 Tellinghuisen T. L. (bi700776eb00015/bi700776eb00015_1) 2005 bi700776eb00051/bi700776eb00051_1 Lohmann V. (bi700776eb00007/bi700776eb00007_1) 1997; 71 Llinas M. (bi700776eb00052/bi700776eb00052_1) 1975; 97 Gong G. (bi700776eb00011/bi700776eb00011_1) 2001 Wang Y. (bi700776eb00039/bi700776eb00039_1) 2002 Brass V. (bi700776eb00013/bi700776eb00013_1) 2002; 277 Dyson H. J. (bi700776eb00042/bi700776eb00042_1) 2002; 12 Shirota Y. (bi700776eb00016/bi700776eb00016_1) 2002; 277 Failla C. (bi700776eb00005/bi700776eb00005_1) 1994; 68 Tompa P. (bi700776eb00041/bi700776eb00041_1) 2002 Tellinghuisen T. L. (bi700776eb00012/bi700776eb00012_1) 2004; 279 Hu Y. (bi700776eb00033/bi700776eb00033_1) 1990; 93 Yeh S. R. (bi700776eb00061/bi700776eb00061_1) 1998 Gale M. J. (bi700776eb00009/bi700776eb00009_1) 1997 Wishart D. S. (bi700776eb00028/bi700776eb00028_1) 2001; 338 Wishart D. S. (bi700776eb00063/bi700776eb00063_1) 1994; 4 Spolar R. S. (bi700776eb00047/bi700776eb00047_1) 1994 Dobson C. M. (bi700776eb00037/bi700776eb00037_1) 1992; 2 Uesugi M. (bi700776eb00050/bi700776eb00050_1) 1997 Ulrich D. L. (bi700776eb00034/bi700776eb00034_1) 2005; 347 Fink A. L. (bi700776eb00056/bi700776eb00056_1) 2005; 15 Blight K. J. (bi700776eb00008/bi700776eb00008_1) 2000 Peti W. (bi700776eb00023/bi700776eb00023_1) 2001; 19 Wright P. E. (bi700776eb00046/bi700776eb00046_1) 1999; 293 Marion D. (bi700776eb00032/bi700776eb00032_1) 1989 Garbuzynskiy S. O. (bi700776eb00062/bi700776eb00062_1) 2004 Nelson J. W. (bi700776eb00053/bi700776eb00053_1) 1986 Adler A. J. (bi700776eb00038/bi700776eb00038_1) 1973 Wishart D. S. (bi700776eb00029/bi700776eb00029_1) 1998 Abbreviations (bi700776en00001/bi700776en00001_1) Thormann T. (bi700776eb00035/bi700776eb00035_1) 2004 Vuister G.W., B. A. (bi700776eb00031/bi700776eb00031_1) 1993; 115 Donaldson L. (bi700776eb00048/bi700776eb00048_1) 1992; 267 Choo Q. L. (bi700776eb00001/bi700776eb00001_1) 1989 Brems D. N. (bi700776eb00059/bi700776eb00059_1) 1986 Vojnic E. (bi700776eb00022/bi700776eb00022_1) 2006; 281 Wishart D. S. (bi700776eb00030/bi700776eb00030_1) 1994 Penin F. (bi700776eb00014/bi700776eb00014_1) 2004; 39 Farrow N. A. (bi700776eb00021/bi700776eb00021_1) 1994 Gunasekaran K. (bi700776eb00045/bi700776eb00045_1) 2003; 28 Miller R. H. (bi700776eb00003/bi700776eb00003_1) 1990 Sonnichsen F. D. (bi700776eb00054/bi700776eb00054_1) 1992 Liang Y. (bi700776eb00058/bi700776eb00058_1) 2006; 22 Uversky V. N. (bi700776eb00044/bi700776eb00044_1) 2002; 269 Uversky V. N. (bi700776eb00057/bi700776eb00057_1) 2002 Merutka G. (bi700776eb00025/bi700776eb00025_1) 1995; 5 Chung Y. L. (bi700776eb00010/bi700776eb00010_1) 2003; 107 Behrens S. E. (bi700776eb00006/bi700776eb00006_1) 1996; 15 Schwalbe H. (bi700776eb00026/bi700776eb00026_1) 1997 bi700776eb00049/bi700776eb00049_1 Street A. (bi700776eb00017/bi700776eb00017_1) 2004; 279 Wootton J. C. (bi700776eb00040/bi700776eb00040_1) 1994 Saito I. (bi700776eb00004/bi700776eb00004_1) 1990 Wishart D. S. (bi700776eb00024/bi700776eb00024_1) 1995; 5 Wishart D. S. (bi700776eb00027/bi700776eb00027_1) 1991; 222 Shiraki K. (bi700776eb00055/bi700776eb00055_1) 1995; 245 Tanimoto A. (bi700776eb00043/bi700776eb00043_1) 1997 Bottomley M. J. (bi700776eb00019/bi700776eb00019_1) 1999; 13 Lavanchy D. (bi700776eb00002/bi700776eb00002_1) 1999; 31 Bhavesh N. S. (bi700776eb00036/bi700776eb00036_1) 2003; 278 |
References_xml | – volume-title: Biochem. Biophys. Res. Commun. 236, 360−364. year: 1997 ident: bi700776eb00043/bi700776eb00043_1 contributor: fullname: Tanimoto A. – volume: 107 start-page: 73 year: 2003 ident: bi700776eb00010/bi700776eb00010_1 publication-title: Int. J. Cancer doi: 10.1002/ijc.11303 contributor: fullname: Chung Y. L. – volume: 278 year: 2003 ident: bi700776eb00036/bi700776eb00036_1 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M301615200 contributor: fullname: Bhavesh N. S. – volume: 338 start-page: 34 year: 2001 ident: bi700776eb00028/bi700776eb00028_1 publication-title: Methods Enzymol. contributor: fullname: Wishart D. S. – volume: 279 year: 2004 ident: bi700776eb00017/bi700776eb00017_1 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M312245200 contributor: fullname: Street A. – ident: bi700776eb00049/bi700776eb00049_1 doi: 10.1126/science.274.5289.948 – volume: 245 year: 1995 ident: bi700776eb00055/bi700776eb00055_1 publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1994.0015 contributor: fullname: Shiraki K. – volume: 13 year: 1999 ident: bi700776eb00019/bi700776eb00019_1 publication-title: J. Biomol. NMR doi: 10.1023/A:1008393903034 contributor: fullname: Bottomley M. J. – volume-title: Methods Enzymol. 239, 363−392. year: 1994 ident: bi700776eb00030/bi700776eb00030_1 contributor: fullname: Wishart D. S. – volume-title: Nature 435, 374−379. year: 2005 ident: bi700776eb00015/bi700776eb00015_1 contributor: fullname: Tellinghuisen T. L. – volume-title: Protein Sci. 11, 852−861. year: 2002 ident: bi700776eb00039/bi700776eb00039_1 contributor: fullname: Wang Y. – volume: 4 year: 1994 ident: bi700776eb00020/bi700776eb00020_1 publication-title: J. Biomol. NMR contributor: fullname: Johnson B. A. B. R. A. – volume: 12 start-page: 60 year: 2002 ident: bi700776eb00042/bi700776eb00042_1 publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/S0959-440X(02)00289-0 contributor: fullname: Dyson H. J. – volume-title: Biochemistry 43, 10364−10369. year: 2004 ident: bi700776eb00035/bi700776eb00035_1 contributor: fullname: Thormann T. – volume: 31 year: 1999 ident: bi700776eb00002/bi700776eb00002_1 publication-title: J. Hepatol. doi: 10.1016/S0168-8278(99)80392-4 contributor: fullname: Lavanchy D. – volume: 15 start-page: 22 year: 1996 ident: bi700776eb00006/bi700776eb00006_1 publication-title: EMBO J. doi: 10.1002/j.1460-2075.1996.tb00329.x contributor: fullname: Behrens S. E. – volume-title: Proc. Natl. Acad. Sci. U.S.A. 98 year: 2001 ident: bi700776eb00011/bi700776eb00011_1 contributor: fullname: Gong G. – volume: 79 year: 2005 ident: bi700776eb00018/bi700776eb00018_1 publication-title: J. Virol. doi: 10.1128/JVI.79.8.5006-5016.2005 contributor: fullname: Street A. – volume-title: Biochem. Cell Biol. 76, 153−163. year: 1998 ident: bi700776eb00029/bi700776eb00029_1 contributor: fullname: Wishart D. S. – volume: 93 year: 1990 ident: bi700776eb00033/bi700776eb00033_1 publication-title: J. Chem. Phys. contributor: fullname: Hu Y. – volume-title: Proc. Natl. Acad. Sci. U.S.A. 87 year: 1990 ident: bi700776eb00003/bi700776eb00003_1 contributor: fullname: Miller R. H. – volume: 269 start-page: 12 year: 2002 ident: bi700776eb00044/bi700776eb00044_1 publication-title: Eur. J. Biochem. doi: 10.1046/j.0014-2956.2001.02649.x contributor: fullname: Uversky V. N. – volume: 277 year: 2002 ident: bi700776eb00013/bi700776eb00013_1 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M111289200 contributor: fullname: Brass V. – volume: 267 year: 1992 ident: bi700776eb00048/bi700776eb00048_1 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)45957-1 contributor: fullname: Donaldson L. – volume: 97 year: 1975 ident: bi700776eb00052/bi700776eb00052_1 publication-title: J. Am. Chem. Soc. doi: 10.1021/ja00849a040 contributor: fullname: Llinas M. – volume: 39 start-page: 19 year: 2004 ident: bi700776eb00014/bi700776eb00014_1 publication-title: Hepatology doi: 10.1002/hep.20032 contributor: fullname: Penin F. – volume: 68 year: 1994 ident: bi700776eb00005/bi700776eb00005_1 publication-title: J. Virol. doi: 10.1128/jvi.68.6.3753-3760.1994 contributor: fullname: Failla C. – volume-title: Protein, Nucleic Acid Enzyme 35, 2117−2127. year: 1990 ident: bi700776eb00004/bi700776eb00004_1 contributor: fullname: Saito I. – volume: 28 start-page: 85 year: 2003 ident: bi700776eb00045/bi700776eb00045_1 publication-title: Trends Biochem. Sci. doi: 10.1016/S0968-0004(03)00003-3 contributor: fullname: Gunasekaran K. – volume-title: Biochemistry 33, 5984−6003. year: 1994 ident: bi700776eb00021/bi700776eb00021_1 contributor: fullname: Farrow N. A. – volume-title: Science 263, 777−784. year: 1994 ident: bi700776eb00047/bi700776eb00047_1 contributor: fullname: Spolar R. S. – volume: 71 year: 1997 ident: bi700776eb00007/bi700776eb00007_1 publication-title: J. Virol. doi: 10.1128/jvi.71.11.8416-8428.1997 contributor: fullname: Lohmann V. – volume-title: Biochemistry 31, 8790−8798. year: 1992 ident: bi700776eb00054/bi700776eb00054_1 contributor: fullname: Sonnichsen F. D. – volume-title: Comput. Chem. 18, 269−285. year: 1994 ident: bi700776eb00040/bi700776eb00040_1 contributor: fullname: Wootton J. C. – volume-title: Biochemistry 29, 11072−11078. year: 1990 ident: bi700776eb00060/bi700776eb00060_1 contributor: fullname: Cleland J. L. – volume: 281 start-page: 15 year: 2006 ident: bi700776eb00022/bi700776eb00022_1 publication-title: J. Biol. Chem. doi: 10.1074/jbc.C500423200 contributor: fullname: Vojnic E. – volume-title: HCV, hepatitis C virus ident: bi700776en00001/bi700776en00001_1 contributor: fullname: Abbreviations – volume: 279 year: 2004 ident: bi700776eb00012/bi700776eb00012_1 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M407787200 contributor: fullname: Tellinghuisen T. L. – volume-title: Nat. Struct. Biol. 5, 222−228. year: 1998 ident: bi700776eb00061/bi700776eb00061_1 contributor: fullname: Yeh S. R. – volume-title: Proteins 1, 211−217. year: 1986 ident: bi700776eb00053/bi700776eb00053_1 contributor: fullname: Nelson J. W. – volume-title: Virology 230, 217−227. year: 1997 ident: bi700776eb00009/bi700776eb00009_1 contributor: fullname: Gale M. J. – ident: bi700776eb00051/bi700776eb00051_1 doi: 10.1006/bbrc.2001.4627 – volume-title: Protein Sci. 11, 739−756. year: 2002 ident: bi700776eb00057/bi700776eb00057_1 contributor: fullname: Uversky V. N. – volume: 347 year: 2005 ident: bi700776eb00034/bi700776eb00034_1 publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2005.01.039 contributor: fullname: Ulrich D. L. – volume-title: Science 277, 1310−1313. year: 1997 ident: bi700776eb00050/bi700776eb00050_1 contributor: fullname: Uesugi M. – volume: 2 start-page: 12 year: 1992 ident: bi700776eb00037/bi700776eb00037_1 publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/0959-440X(92)90169-8 contributor: fullname: Dobson C. M. – volume-title: Trends Biochem. Sci. 27, 527−533. year: 2002 ident: bi700776eb00041/bi700776eb00041_1 contributor: fullname: Tompa P. – volume-title: Protein Sci. 13, 2871−2877. year: 2004 ident: bi700776eb00062/bi700776eb00062_1 contributor: fullname: Garbuzynskiy S. O. – volume-title: Science 290 year: 2000 ident: bi700776eb00008/bi700776eb00008_1 contributor: fullname: Blight K. J. – volume-title: Biochemistry 36, 8977−8991. year: 1997 ident: bi700776eb00026/bi700776eb00026_1 contributor: fullname: Schwalbe H. – volume: 293 year: 1999 ident: bi700776eb00046/bi700776eb00046_1 publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1999.3110 contributor: fullname: Wright P. E. – volume-title: Biochemistry 25, 6539−6543. year: 1986 ident: bi700776eb00059/bi700776eb00059_1 contributor: fullname: Brems D. N. – volume: 19 year: 2001 ident: bi700776eb00023/bi700776eb00023_1 publication-title: J. Biomol. NMR doi: 10.1023/A:1008307323283 contributor: fullname: Peti W. – volume: 4 year: 1994 ident: bi700776eb00063/bi700776eb00063_1 publication-title: J. Biomol. NMR doi: 10.1007/BF00175245 contributor: fullname: Wishart D. S. – volume: 115 year: 1993 ident: bi700776eb00031/bi700776eb00031_1 publication-title: J. Am. Chem. Soc. contributor: fullname: Vuister G.W., B. A. – volume: 5 start-page: 24 year: 1995 ident: bi700776eb00025/bi700776eb00025_1 publication-title: J. Biomol. NMR doi: 10.1007/BF00227466 contributor: fullname: Merutka G. – volume: 222 year: 1991 ident: bi700776eb00027/bi700776eb00027_1 publication-title: J. Mol. Biol. doi: 10.1016/0022-2836(91)90214-Q contributor: fullname: Wishart D. S. – volume-title: Biochemistry 28, 6150−6156. year: 1989 ident: bi700776eb00032/bi700776eb00032_1 contributor: fullname: Marion D. – volume: 15 start-page: 41 year: 2005 ident: bi700776eb00056/bi700776eb00056_1 publication-title: Curr. Opin. Struct. Biol. contributor: fullname: Fink A. L. – volume: 5 start-page: 81 year: 1995 ident: bi700776eb00024/bi700776eb00024_1 publication-title: J. Biomol. NMR doi: 10.1007/BF00227471 contributor: fullname: Wishart D. S. – volume-title: Methods Enzymol. 27, 675−735. year: 1973 ident: bi700776eb00038/bi700776eb00038_1 contributor: fullname: Adler A. J. – volume-title: Science 244, 359−362. year: 1989 ident: bi700776eb00001/bi700776eb00001_1 contributor: fullname: Choo Q. L. – volume: 277 year: 2002 ident: bi700776eb00016/bi700776eb00016_1 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M111392200 contributor: fullname: Shirota Y. – volume: 22 start-page: 20 year: 2006 ident: bi700776eb00058/bi700776eb00058_1 publication-title: Mol. Cells doi: 10.1016/S1016-8478(23)17385-7 contributor: fullname: Liang Y. |
SSID | ssj0004074 |
Score | 2.236245 |
Snippet | Nonstructural protein 5A protein (NS5A) of hepatitis C virus (HCV) plays an important role in the regulation of viral replication, interferon resistance, and... |
SourceID | proquest crossref pubmed istex acs |
SourceType | Aggregation Database Index Database Publisher |
StartPage | 11550 |
SubjectTerms | Amino Acid Sequence Apoptosis Hepacivirus - chemistry Hepacivirus - physiology Hepatitis C virus Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Peptide Fragments - chemistry Protein Conformation Protein Denaturation Protein Folding Recombinant Proteins - chemistry Recombinant Proteins - metabolism Viral Nonstructural Proteins - chemistry Viral Nonstructural Proteins - genetics Viral Nonstructural Proteins - metabolism Virus Replication |
Title | Domain 2 of Nonstructural Protein 5A (NS5A) of Hepatitis C Virus Is Natively Unfolded |
URI | http://dx.doi.org/10.1021/bi700776e https://api.istex.fr/ark:/67375/TPS-8M2V9MV1-6/fulltext.pdf https://www.ncbi.nlm.nih.gov/pubmed/17880107 https://search.proquest.com/docview/20561704 https://search.proquest.com/docview/68361205 |
Volume | 46 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwhV1Rb9MwED6N7QFeYGwwCtuwAE3wkBEntuM8Vh1TQWo1qWu1N8uxHanalqCllRi_nrObbENQeM5FcnyXu--zz58BPiRMU2M4jSgveIT1VkYypzqSxvp2sdi5sKY7GovhlH274Bcb8H7NDn5CPxfzLGjOuEewlWRIuz3-GUzuDz_GrdQyUuME8XgnH_TwVV96TPNb6dnys_hjPa4M9eX0GZx0p3RWbSWXx8tFcWx-_ina-K-hb8PTFl-S_iognsOGq3Zgt18ht76-JUckdHyGpfQdeDzobnvbhelJfa3nFUlIXZJx3erKek0OcualHPAR75OP4wnvf_ImQ-dbsRfzhgzIbH6zbMjXhoyDivjVLZli2F5ZZ1_A9PTL-WAYtVcuRBp52iISlmmrS8stpgIeMwQXwtf4XNvYpHkpPQGUhaBCGJdr6SS33KVZgXmTWcfSl7BZ1ZV7BYRaIx0aGyoky8s05yXLDUVEYhBiFLIHh-gT1f4yjQq74QlVd5PWg3edu9T3lfTG34yOgiPvLPTNpe9Vy7g6P5soOUpm-WhGlejB287TCqfWb4voytXLRiWeRGUxW28hZIpAMOY92FuFyP14Msx_yKBf_-9j3sCTsCrse2HEPmyiE90BwplFcRjC-Re8c-jq |
link.rule.ids | 314,780,784,2765,27076,27924,27925,56738,56788 |
linkProvider | American Chemical Society |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV1Lb9QwEB5BeygXHi2P5dFaCFVwSIkT23GOq4VqC92o0j7Um-XYjrRqm6BmV6L8esbebBcQFZwzieyZiecbe_wNwLuEaWoMpxHlJY8w3spI5lRH0lhfLhY7F_Z0R4UYTtmXc37e0eT4uzA4iBa_1IZD_A27AP1YzrNAPePuwzb3rSo9DBqMN3cg445xGTPkBGH5mkXo11d9BDLtbxFo2yvz-93wMoSZ40erfkVhgKG65OJouSiPzI8_uBv_bwaP4WGHNkl_5R5P4J6rd2GvX2OmfXVDDkmo_wwb67uwM1j3ftuD6afmSs9rkpCmIkXTscx6hg5y5okd8BHvk_fFmPc_eJGh84XZi3lLBmQ2v1625KQlReAUv7whU3TiS-vsU5gef54MhlHXgCHSmLUtImGZtrqy3OLCwGOGUEP4iJ9rG5s0r6RPB2UpqBDG5Vo6yS13aVbiKsqsY-kz2Kqb2r0AQq2RDoUNFZLlVZrziuWGIj4xCDhK2YN91JnqfqBWhbPxhKpbpfXg7dpq6tuKiONvQofBnrcS-vrCV65lXE3OxkqOklk-mlElenCwNrhC1fpDEl27ZtmqxKdUWczulhAyRVgY8x48X3nKZjwZroaYT7_812QOYGc4GZ2q05Pi6yt4EPaLfZWMeA1baFD3BoHOotwPHv4TrxfxVw |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV3db9MwED_BJgEvfGx8lI_NQmiCh4w4iR3nMeqoOqChUtdqb5ZjO1K1LZmWVmL89ZzdtAPEBM-5WPbd2fc7-_wzwLsoUVRrRgPKShZgvBWByKgKhDauXCy01u_pjgo-nCafT9lplyi6uzDYiRZbav0hvpvVl6bqGAbox3KeevoZexe2Ga6yroQr709u7kGGHesyZskRQvM1k9Cvv7oopNvfotC2U-j32yGmDzWDR_Bt00lfYXJ2uFyUh_rHH_yN_z-Kx_CwQ50kX7nJE7hj6x3YzWvMuC-uyQHxdaB-g30H7vfXb8DtwvSouVDzmkSkqUjRdGyzjqmDjB3BA35iOXlfTFj-wYkMrSvQXsxb0iez-dWyJcctKTy3-Pk1maIznxtrnsJ08OmkPwy6hxgChdnbIuAmUUZVhhlcIFiYIOTgLvJnyoQ6zirh0kJRcsq5tpkSVjDDbJyWuJomxibxM9iqm9q-AEKNFhaFNeUiyao4Y1WSaYo4RSPwKEUP9lBvsptIrfRn5BGVG6X14O3acvJyRcjxN6EDb9ONhLo6cxVsKZMn44kUo2iWjWZU8h7sr40uUbXusETVtlm2MnKpVRomt0twESM8DFkPnq-85aY_6JqY56Yv_zWYfbg3PhrIr8fFl1fwwG8bu2IZ_hq20J72DeKdRbnnnfwnv_bz2g |
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=Domain+2+of+Nonstructural+Protein+5A+%28NS5A%29+of+Hepatitis+C+Virus+Is+Natively+Unfolded&rft.jtitle=Biochemistry+%28Easton%29&rft.au=Liang%2C+Yu&rft.au=Ye%2C+Hong&rft.au=Kang%2C+Cong+Bao&rft.au=Yoon%2C+Ho+Sup&rft.date=2007-10-16&rft.issn=0006-2960&rft.eissn=1520-4995&rft.volume=46&rft.issue=41&rft.spage=11550&rft.epage=11558&rft_id=info:doi/10.1021%2Fbi700776e&rft.externalDBID=n%2Fa&rft.externalDocID=10_1021_bi700776e |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0006-2960&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0006-2960&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0006-2960&client=summon |