An Atomic Model of the Tropomyosin Cable on F-actin
Tropomyosin regulates a wide variety of actin filament functions and is best known for the role that it plays together with troponin in controlling muscle activity. For effective performance on actin filaments, adjacent 42-nm-long tropomyosin molecules are joined together by a 9- to 10-residue head-...
Saved in:
Published in | Biophysical journal Vol. 107; no. 3; pp. 694 - 699 |
---|---|
Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
05.08.2014
Biophysical Society The Biophysical Society |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Tropomyosin regulates a wide variety of actin filament functions and is best known for the role that it plays together with troponin in controlling muscle activity. For effective performance on actin filaments, adjacent 42-nm-long tropomyosin molecules are joined together by a 9- to 10-residue head-to-tail overlapping domain to form a continuous cable that wraps around the F-actin helix. Yet, despite the apparent simplicity of tropomyosin’s coiled-coil structure and its well-known periodic association with successive actin subunits along F-actin, the structure of the tropomyosin cable on actin is uncertain. This is because the conformation of the overlap region that joins neighboring molecules is poorly understood, thus leaving a significant gap in our understanding of thin-filament structure and regulation. However, recent molecular-dynamics simulations of overlap segments defined their overall shape and provided unique and sufficient cues to model the whole actin-tropomyosin filament assembly in atomic detail. In this study, we show that these MD structures merge seamlessly onto the ends of tropomyosin coiled-coils. Adjacent tropomyosin molecules can then be joined together to provide a comprehensive model of the tropomyosin cable running continuously on F-actin. The resulting complete model presented here describes for the first time (to our knowledge) an atomic-level structure of αα-striated muscle tropomyosin bound to an actin filament that includes the critical overlap domain. Thus, the model provides a structural correlate to evaluate thin-filament mechanics, self-assembly mechanisms, and the effect of disease-causing mutations. |
---|---|
AbstractList | Tropomyosin regulates a wide variety of actin filament functions and is best known for the role that it plays together with troponin in controlling muscle activity. For effective performance on actin filaments, adjacent 42-nm-long tropomyosin molecules are joined together by a 9- to 10-residue head-to-tail overlapping domain to form a continuous cable that wraps around the F-actin helix. Yet, despite the apparent simplicity of tropomyosin's coiled-coil structure and its well-known periodic association with successive actin subunits along F-actin, the structure of the tropomyosin cable on actin is uncertain. This is because the conformation of the overlap region that joins neighboring molecules is poorly understood, thus leaving a significant gap in our understanding of thin-filament structure and regulation. However, recent molecular-dynamics simulations of overlap segments defined their overall shape and provided unique and sufficient cues to model the whole actin-tropomyosin filament assembly in atomic detail. In this study, we show that these MD structures merge seamlessly onto the ends of tropomyosin coiled-coils. Adjacent tropomyosin molecules can then be joined together to provide a comprehensive model of the tropomyosin cable running continuously on F-actin. The resulting complete model presented here describes for the first time (to our knowledge) an atomic-level structure of αα-striated muscle tropomyosin bound to an actin filament that includes the critical overlap domain. Thus, the model provides a structural correlate to evaluate thin-filament mechanics, self-assembly mechanisms, and the effect of disease-causing mutations. Tropomyosin regulates a wide variety of actin filament functions and is best known for the role that it plays together with troponin in controlling muscle activity. For effective performance on actin filaments, adjacent 42-nm-long tropomyosin molecules are joined together by a 9- to 10-residue head-to-tail overlapping domain to form a continuous cable that wraps around the F-actin helix. Yet, despite the apparent simplicity of tropomyosin’s coiled-coil structure and its well-known periodic association with successive actin subunits along F-actin, the structure of the tropomyosin cable on actin is uncertain. This is because the conformation of the overlap region that joins neighboring molecules is poorly understood, thus leaving a significant gap in our understanding of thin-filament structure and regulation. However, recent molecular-dynamics simulations of overlap segments defined their overall shape and provided unique and sufficient cues to model the whole actin-tropomyosin filament assembly in atomic detail. In this study, we show that these MD structures merge seamlessly onto the ends of tropomyosin coiled-coils. Adjacent tropomyosin molecules can then be joined together to provide a comprehensive model of the tropomyosin cable running continuously on F-actin. The resulting complete model presented here describes for the first time (to our knowledge) an atomic-level structure of αα -striated muscle tropomyosin bound to an actin filament that includes the critical overlap domain. Thus, the model provides a structural correlate to evaluate thin-filament mechanics, self-assembly mechanisms, and the effect of disease-causing mutations. |
Author | Lehman, William Orzechowski, Marek Fischer, Stefan Li, Xiaochuan (Edward) |
AuthorAffiliation | 1 Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts 2 Computational Biochemistry Group, Interdisciplinary Center for Scientific Computing (IWR), University of Heidelberg, Heidelberg, Germany |
AuthorAffiliation_xml | – name: 1 Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts – name: 2 Computational Biochemistry Group, Interdisciplinary Center for Scientific Computing (IWR), University of Heidelberg, Heidelberg, Germany |
Author_xml | – sequence: 1 givenname: Marek surname: Orzechowski fullname: Orzechowski, Marek organization: Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts – sequence: 2 givenname: Xiaochuan (Edward) surname: Li fullname: Li, Xiaochuan (Edward) organization: Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts – sequence: 3 givenname: Stefan surname: Fischer fullname: Fischer, Stefan email: stefan.fischer@iwr.uni-heidelberg.de organization: Computational Biochemistry Group, Interdisciplinary Center for Scientific Computing (IWR), University of Heidelberg, Heidelberg, Germany – sequence: 4 givenname: William surname: Lehman fullname: Lehman, William email: wlehman@bu.edu organization: Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/25099808$$D View this record in MEDLINE/PubMed |
BookMark | eNp9kU1v1DAQhi1URLeFH8AFReLCJWEcf8QWEtJqRQGpiMveLceZUEeJvdjZSv33eLWlAg6c5uBn3pnxc0UuQgxIyGsKDQUq309Nf5iaFihvQDbA-DOyoYK3NYCSF2QDALJmXItLcpXzBEBbAfQFuSxFawVqQ9g2VNs1Lt5V3-KAcxXHar3Dap_iIS4PMftQ7Ww_YxVDdVNbt_rwkjwf7Zzx1WO9JvubT_vdl_r2--evu-1t7QQXa62GYaStowrKUN1L19m-033XaemEBMf5YMXQat2LkYFqOwv9gMgRFTKt2DX5eI49HPsFB4dhTXY2h-QXmx5MtN78_RL8nfkR7w2nrRYAJeDdY0CKP4-YV7P47HCebcB4zIYK0TKpFOsK-vYfdIrHFMp1J4rRjkndFoqeKZdizgnHp2UomJMRM5lixJyMGJCmGCk9b_684qnjt4ICfDgDWL7y3mMy2XkMDgef0K1miP4_8b8AyX2b3A |
CitedBy_id | crossref_primary_10_1039_C6CP02610A crossref_primary_10_1371_journal_pbio_3000848 crossref_primary_10_1113_JP276741 crossref_primary_10_1085_jgp_202012640 crossref_primary_10_3389_fphys_2022_932333 crossref_primary_10_1021_acs_biochem_7b00266 crossref_primary_10_1073_pnas_1903228116 crossref_primary_10_1134_S0022093021030133 crossref_primary_10_3390_ijms232416223 crossref_primary_10_1085_jgp_201812188 crossref_primary_10_1007_s10974_015_9419_z crossref_primary_10_1085_jgp_202413538 crossref_primary_10_1074_jbc_RA118_005098 crossref_primary_10_1038_s41598_019_47592_9 crossref_primary_10_3390_ijms23105306 crossref_primary_10_1016_j_abb_2018_04_002 crossref_primary_10_1074_jbc_RA120_015277 crossref_primary_10_1085_jgp_202213274 crossref_primary_10_1016_j_abb_2016_02_016 crossref_primary_10_1073_pnas_1519541113 crossref_primary_10_1016_j_isci_2022_104484 crossref_primary_10_1002_ana_24535 crossref_primary_10_3390_ijms22084036 crossref_primary_10_1016_j_ijbiomac_2018_09_105 crossref_primary_10_1016_j_lssr_2023_03_001 crossref_primary_10_1002_pro_4000 crossref_primary_10_1016_j_abb_2014_09_007 crossref_primary_10_1016_j_bpj_2020_05_017 crossref_primary_10_1016_j_bpj_2015_06_006 crossref_primary_10_1091_mbc_E19_10_0586 crossref_primary_10_1096_fj_201800755R crossref_primary_10_1063_1_4940223 crossref_primary_10_1016_j_abb_2016_09_008 crossref_primary_10_1016_j_bbrc_2018_02_172 crossref_primary_10_1016_j_bpj_2019_11_3396 crossref_primary_10_1007_s10974_019_09501_5 crossref_primary_10_1016_j_bpj_2019_11_3393 crossref_primary_10_1085_jgp_202313387 crossref_primary_10_1021_acs_biochem_0c00416 crossref_primary_10_1016_j_bpj_2019_05_009 crossref_primary_10_1016_j_abb_2015_02_026 crossref_primary_10_1016_j_jsb_2017_01_004 crossref_primary_10_1073_pnas_2001692117 |
Cites_doi | 10.1002/jcc.21287 10.1021/bi100349a 10.1016/S0021-9258(17)43316-3 10.1073/pnas.102179999 10.1016/S1937-6448(10)81003-2 10.1007/978-0-387-85766-4_5 10.1016/j.bbrc.2014.02.097 10.1152/physrev.2000.80.2.853 10.1016/j.bpj.2010.12.3697 10.1016/0263-7855(96)00018-5 10.1093/hmg/ddt345 10.1002/jcc.20289 10.1007/s10974-013-9358-5 10.1016/j.abb.2014.01.001 10.1016/S0065-3233(04)71004-9 10.1016/j.jmb.2006.08.033 10.1016/j.abb.2013.09.011 10.1007/s10974-008-9157-6 10.1016/j.bpj.2010.05.004 10.1016/j.tcb.2005.04.007 10.1074/jbc.M113.451161 |
ContentType | Journal Article |
Copyright | 2014 Biophysical Society Copyright © 2014 Biophysical Society. Published by Elsevier Inc. All rights reserved. Copyright Biophysical Society Aug 5, 2014 2014 by the Biophysical Society. 2014 Biophysical Society |
Copyright_xml | – notice: 2014 Biophysical Society – notice: Copyright © 2014 Biophysical Society. Published by Elsevier Inc. All rights reserved. – notice: Copyright Biophysical Society Aug 5, 2014 – notice: 2014 by the Biophysical Society. 2014 Biophysical Society |
DBID | 6I. AAFTH CGR CUY CVF ECM EIF NPM AAYXX CITATION 7QO 7QP 7TK 7TM 7U9 8FD FR3 H94 K9. P64 7X8 5PM |
DOI | 10.1016/j.bpj.2014.06.034 |
DatabaseName | ScienceDirect Open Access Titles Elsevier:ScienceDirect:Open Access Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef Biotechnology Research Abstracts Calcium & Calcified Tissue Abstracts Neurosciences Abstracts Nucleic Acids Abstracts Virology and AIDS Abstracts Technology Research Database Engineering Research Database AIDS and Cancer Research Abstracts ProQuest Health & Medical Complete (Alumni) Biotechnology and BioEngineering Abstracts MEDLINE - Academic PubMed Central (Full Participant titles) |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef Virology and AIDS Abstracts Biotechnology Research Abstracts Technology Research Database Nucleic Acids Abstracts AIDS and Cancer Research Abstracts ProQuest Health & Medical Complete (Alumni) Engineering Research Database Calcium & Calcified Tissue Abstracts Neurosciences Abstracts Biotechnology and BioEngineering Abstracts MEDLINE - Academic |
DatabaseTitleList | MEDLINE Virology and AIDS Abstracts |
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 | Biology |
EISSN | 1542-0086 |
EndPage | 699 |
ExternalDocumentID | 3402547491 10_1016_j_bpj_2014_06_034 25099808 S000634951400678X |
Genre | Journal Article Research Support, N.I.H., Extramural |
GrantInformation_xml | – fundername: NHLBI NIH HHS grantid: R37-HL036153 – fundername: NHLBI NIH HHS grantid: R37 HL036153 |
GroupedDBID | --- -DZ -~X .55 0R~ 23N 2WC 4.4 457 5GY 5RE 62- 6I. 6J9 AACTN AAEDT AAEDW AAFTH AAIAV AAKRW AALRI AAUCE AAVLU AAXJY AAXUO ABJNI ABMAC ABMWF ABVKL ACBEA ACGFO ACGFS ACGOD ACIWK ACNCT ACPRK ADBBV ADEZE ADJPV AENEX AEXQZ AFRAH AFTJW AGHFR AGKMS AHMBA AHPSJ AITUG ALKID ALMA_UNASSIGNED_HOLDINGS AMRAJ AOIJS AYCSE AZFZN BAWUL CS3 D0L DIK DU5 E3Z EBS EJD F5P FCP FDB FRP HYE IH2 IXB JIG KQ8 L7B M41 N9A NCXOZ O-L O9- OK1 P2P RCE RIG RNS ROL RPM RWL SES SSZ TAE TBP TN5 WH7 WOQ WOW WQ6 X7M YNY YWH ZA5 ~02 0SF AAMRU ADVLN AKAPO AKRWK ALIPV CGR CUY CVF ECM EIF NPM --K .GJ 3O- 3V. 53G 6TJ 7X2 7X7 88A 88E 88I 8AF 8AO 8FE 8FG 8FH 8FI 8FJ 8G5 8R4 8R5 AAIKJ AAQXK AAYXX ABUWG ACRPL ADMUD AFKRA AI. ARAPS ASPBG ATCPS AVWKF AZQEC BBNVY BENPR BGLVJ BHPHI BPHCQ BVXVI CCPQU CITATION DWQXO FEDTE FGOYB FYUFA G-2 GNUQQ GUQSH GX1 H13 HCIFZ HMCUK HVGLF HX~ HZ~ LK8 M0K M0L M1P M2O M2P M2Q M7P MVM OZT P62 PQQKQ PRG PROAC PSQYO Q2X R2- S0X UKHRP UKR VH1 YYP ZGI ZXP ~KM 7QO 7QP 7TK 7TM 7U9 8FD FR3 H94 K9. P64 7X8 5PM |
ID | FETCH-LOGICAL-c545t-8ddf12c1805019b6c7ab79b7796c560c44da5d299b5f30827a0bdee4ee8e3983 |
IEDL.DBID | RPM |
ISSN | 0006-3495 |
IngestDate | Tue Sep 17 21:23:28 EDT 2024 Fri Oct 25 21:46:39 EDT 2024 Thu Oct 10 17:22:49 EDT 2024 Fri Dec 06 04:59:24 EST 2024 Sat Sep 28 08:05:47 EDT 2024 Fri Feb 23 02:27:14 EST 2024 |
IsDoiOpenAccess | true |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 3 |
Language | English |
License | http://www.elsevier.com/open-access/userlicense/1.0 Copyright © 2014 Biophysical Society. Published by Elsevier Inc. All rights reserved. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c545t-8ddf12c1805019b6c7ab79b7796c560c44da5d299b5f30827a0bdee4ee8e3983 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
OpenAccessLink | https://www.sciencedirect.com/science/article/pii/S000634951400678X |
PMID | 25099808 |
PQID | 1553173692 |
PQPubID | 7454 |
PageCount | 6 |
ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_4129500 proquest_miscellaneous_1552368837 proquest_journals_1553173692 crossref_primary_10_1016_j_bpj_2014_06_034 pubmed_primary_25099808 elsevier_sciencedirect_doi_10_1016_j_bpj_2014_06_034 |
PublicationCentury | 2000 |
PublicationDate | 2014-08-05 |
PublicationDateYYYYMMDD | 2014-08-05 |
PublicationDate_xml | – month: 08 year: 2014 text: 2014-08-05 day: 05 |
PublicationDecade | 2010 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States – name: New York |
PublicationTitle | Biophysical journal |
PublicationTitleAlternate | Biophys J |
PublicationYear | 2014 |
Publisher | Elsevier Inc Biophysical Society The Biophysical Society |
Publisher_xml | – name: Elsevier Inc – name: Biophysical Society – name: The Biophysical Society |
References | Humphrey, Dalke, Schulten (bib14) 1996; 14 Barua, Fagnant, Hitchcock-DeGregori (bib8) 2013; 288 Li, Orzechowski, Fischer (bib10) 2014; 446 Greenfield, Huang, Hitchcock-DeGregori (bib11) 2006; 364 Frye, Klenchin, Rayment (bib12) 2010; 49 Holmes, Lehman (bib2) 2008; 29 Phillips, Braun, Schulten (bib16) 2005; 26 Sousa, Cammarato, Lehman (bib18) 2010; 99 Hitchcock-DeGregori (bib6) 2008; 644 Brown, Cohen (bib1) 2005; 71 Orzechowski, Moore, Lehman (bib9) 2014; 545 Lehrer, Morris (bib19) 1984; 259 Gordon, Homsher, Regnier (bib3) 2000; 80 Li, Mui, Cohen (bib17) 2002; 99 Wang, Coluccio (bib5) 2010; 281 Brooks, Brooks, Karplus (bib15) 2009; 30 Lehman, Li, Fischer (bib13) 2014; 552-553 Marston, Memo, Lehman (bib21) 2013; 22 Li, Tobacman, Lehman (bib7) 2011; 100 Gunning, Schevzov, Hardeman (bib4) 2005; 15 Redwood, Robinson (bib20) 2013; 34 23886664 - Hum Mol Genet. 2013 Dec 15;22(24):4978-87 20682264 - Biophys J. 2010 Aug 4;99(3):862-8 19209813 - Adv Exp Med Biol. 2008;644:60-72 24607906 - Biochem Biophys Res Commun. 2014 Mar 28;446(1):304-8 10747208 - Physiol Rev. 2000 Apr;80(2):853-924 19444816 - J Comput Chem. 2009 Jul 30;30(10):1545-614 12032291 - Proc Natl Acad Sci U S A. 2002 May 28;99(11):7378-83 19116763 - J Muscle Res Cell Motil. 2008;29(6-8):213-9 16999976 - J Mol Biol. 2006 Nov 17;364(1):80-96 24071513 - Arch Biochem Biophys. 2014 Jun 15;552-553:68-73 8744570 - J Mol Graph. 1996 Feb;14(1):33-8, 27-8 15953552 - Trends Cell Biol. 2005 Jun;15(6):333-41 16230111 - Adv Protein Chem. 2005;71:121-59 20460184 - Int Rev Cell Mol Biol. 2010;281:91-128 6230348 - J Biol Chem. 1984 Feb 25;259(4):2070-2 24412204 - Arch Biochem Biophys. 2014 Mar 1;545:63-8 20465283 - Biochemistry. 2010 Jun 15;49(23):4908-20 16222654 - J Comput Chem. 2005 Dec;26(16):1781-802 21320445 - Biophys J. 2011 Feb 16;100(4):1005-13 23420843 - J Biol Chem. 2013 Apr 5;288(14):9602-9 24005378 - J Muscle Res Cell Motil. 2013 Aug;34(3-4):285-94 Brown (10.1016/j.bpj.2014.06.034_bib1) 2005; 71 Humphrey (10.1016/j.bpj.2014.06.034_bib14) 1996; 14 Brooks (10.1016/j.bpj.2014.06.034_bib15) 2009; 30 Barua (10.1016/j.bpj.2014.06.034_bib8) 2013; 288 Lehrer (10.1016/j.bpj.2014.06.034_bib19) 1984; 259 Li (10.1016/j.bpj.2014.06.034_bib17) 2002; 99 Sousa (10.1016/j.bpj.2014.06.034_bib18) 2010; 99 Marston (10.1016/j.bpj.2014.06.034_bib21) 2013; 22 Gordon (10.1016/j.bpj.2014.06.034_bib3) 2000; 80 Gunning (10.1016/j.bpj.2014.06.034_bib4) 2005; 15 Lehman (10.1016/j.bpj.2014.06.034_bib13) 2014; 552-553 Wang (10.1016/j.bpj.2014.06.034_bib5) 2010; 281 Phillips (10.1016/j.bpj.2014.06.034_bib16) 2005; 26 Frye (10.1016/j.bpj.2014.06.034_bib12) 2010; 49 Li (10.1016/j.bpj.2014.06.034_bib10) 2014; 446 Orzechowski (10.1016/j.bpj.2014.06.034_bib9) 2014; 545 Hitchcock-DeGregori (10.1016/j.bpj.2014.06.034_bib6) 2008; 644 Redwood (10.1016/j.bpj.2014.06.034_bib20) 2013; 34 Greenfield (10.1016/j.bpj.2014.06.034_bib11) 2006; 364 Holmes (10.1016/j.bpj.2014.06.034_bib2) 2008; 29 Li (10.1016/j.bpj.2014.06.034_bib7) 2011; 100 |
References_xml | – volume: 281 start-page: 91 year: 2010 end-page: 128 ident: bib5 article-title: New insights into the regulation of the actin cytoskeleton by tropomyosin publication-title: Int. Rev. Cell Mol. Biol contributor: fullname: Coluccio – volume: 446 start-page: 304 year: 2014 end-page: 308 ident: bib10 article-title: Structure and flexibility of the tropomyosin overlap junction publication-title: Biochem. Biophys. Res. Commun. contributor: fullname: Fischer – volume: 545 start-page: 63 year: 2014 end-page: 68 ident: bib9 article-title: Tropomyosin movement on F-actin during muscle activation explained by energy landscapes publication-title: Arch. Biochem. Biophys. contributor: fullname: Lehman – volume: 80 start-page: 853 year: 2000 end-page: 924 ident: bib3 article-title: Regulation of contraction in striated muscle publication-title: Physiol. Rev. contributor: fullname: Regnier – volume: 49 start-page: 4908 year: 2010 end-page: 4920 ident: bib12 article-title: Structure of the tropomyosin overlap complex from chicken smooth muscle: insight into the diversity of N-terminal recognition publication-title: Biochemistry contributor: fullname: Rayment – volume: 34 start-page: 285 year: 2013 end-page: 294 ident: bib20 article-title: -Tropomyosin mutations in inherited cardiomyopathies publication-title: J. Muscle Res. Cell Motil. contributor: fullname: Robinson – volume: 644 start-page: 60 year: 2008 end-page: 72 ident: bib6 article-title: Tropomyosin: function follows structure publication-title: Adv. Exp. Med. Biol. contributor: fullname: Hitchcock-DeGregori – volume: 288 start-page: 9602 year: 2013 end-page: 9609 ident: bib8 article-title: A periodic pattern of evolutionarily conserved basic and acidic residues constitutes the binding interface of actin-tropomyosin publication-title: J. Biol. Chem. contributor: fullname: Hitchcock-DeGregori – volume: 26 start-page: 1781 year: 2005 end-page: 1802 ident: bib16 article-title: Scalable molecular dynamics with NAMD publication-title: J. Comput. Chem. contributor: fullname: Schulten – volume: 552-553 start-page: 68 year: 2014 end-page: 73 ident: bib13 article-title: The structural dynamics of publication-title: Arch. Biochem. Biophys. contributor: fullname: Fischer – volume: 30 start-page: 1545 year: 2009 end-page: 1614 ident: bib15 article-title: CHARMM: the biomolecular simulation program publication-title: J. Comput. Chem. contributor: fullname: Karplus – volume: 15 start-page: 333 year: 2005 end-page: 341 ident: bib4 article-title: Tropomyosin isoforms: divining rods for actin cytoskeleton function publication-title: Trends Cell Biol. contributor: fullname: Hardeman – volume: 99 start-page: 7378 year: 2002 end-page: 7383 ident: bib17 article-title: The crystal structure of the C-terminal fragment of striated-muscle publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Cohen – volume: 364 start-page: 80 year: 2006 end-page: 96 ident: bib11 article-title: Solution NMR structure of the junction between tropomyosin molecules: implications for actin binding and regulation publication-title: J. Mol. Biol. contributor: fullname: Hitchcock-DeGregori – volume: 14 start-page: 33 year: 1996 end-page: 38 ident: bib14 article-title: VMD: visual molecular dynamics publication-title: J. Mol. Graph. contributor: fullname: Schulten – volume: 29 start-page: 213 year: 2008 end-page: 219 ident: bib2 article-title: Gestalt-binding of tropomyosin to actin filaments publication-title: J. Muscle Res. Cell Motil. contributor: fullname: Lehman – volume: 259 start-page: 2070 year: 1984 end-page: 2072 ident: bib19 article-title: Comparison of the effects of smooth and skeletal tropomyosin on skeletal actomyosin subfragment 1 ATPase publication-title: J. Biol. Chem. contributor: fullname: Morris – volume: 71 start-page: 121 year: 2005 end-page: 159 ident: bib1 article-title: Regulation of muscle contraction by tropomyosin and troponin: how structure illuminates function publication-title: Adv. Protein Chem. contributor: fullname: Cohen – volume: 22 start-page: 4978 year: 2013 end-page: 4987 ident: bib21 article-title: Mutations in repeating structural motifs of tropomyosin cause gain of function in skeletal muscle myopathy patients publication-title: Hum. Mol. Genet. contributor: fullname: Lehman – volume: 99 start-page: 862 year: 2010 end-page: 868 ident: bib18 article-title: Electron microscopy and persistence length analysis of semi-rigid smooth muscle tropomyosin strands publication-title: Biophys. J. contributor: fullname: Lehman – volume: 100 start-page: 1005 year: 2011 end-page: 1013 ident: bib7 article-title: Tropomyosin position on F-actin revealed by EM reconstruction and computational chemistry publication-title: Biophys. J. contributor: fullname: Lehman – volume: 30 start-page: 1545 year: 2009 ident: 10.1016/j.bpj.2014.06.034_bib15 article-title: CHARMM: the biomolecular simulation program publication-title: J. Comput. Chem. doi: 10.1002/jcc.21287 contributor: fullname: Brooks – volume: 49 start-page: 4908 year: 2010 ident: 10.1016/j.bpj.2014.06.034_bib12 article-title: Structure of the tropomyosin overlap complex from chicken smooth muscle: insight into the diversity of N-terminal recognition publication-title: Biochemistry doi: 10.1021/bi100349a contributor: fullname: Frye – volume: 259 start-page: 2070 year: 1984 ident: 10.1016/j.bpj.2014.06.034_bib19 article-title: Comparison of the effects of smooth and skeletal tropomyosin on skeletal actomyosin subfragment 1 ATPase publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)43316-3 contributor: fullname: Lehrer – volume: 99 start-page: 7378 year: 2002 ident: 10.1016/j.bpj.2014.06.034_bib17 article-title: The crystal structure of the C-terminal fragment of striated-muscle α-tropomyosin reveals a key troponin T recognition site publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.102179999 contributor: fullname: Li – volume: 281 start-page: 91 year: 2010 ident: 10.1016/j.bpj.2014.06.034_bib5 article-title: New insights into the regulation of the actin cytoskeleton by tropomyosin publication-title: Int. Rev. Cell Mol. Biol doi: 10.1016/S1937-6448(10)81003-2 contributor: fullname: Wang – volume: 644 start-page: 60 year: 2008 ident: 10.1016/j.bpj.2014.06.034_bib6 article-title: Tropomyosin: function follows structure publication-title: Adv. Exp. Med. Biol. doi: 10.1007/978-0-387-85766-4_5 contributor: fullname: Hitchcock-DeGregori – volume: 446 start-page: 304 year: 2014 ident: 10.1016/j.bpj.2014.06.034_bib10 article-title: Structure and flexibility of the tropomyosin overlap junction publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2014.02.097 contributor: fullname: Li – volume: 80 start-page: 853 year: 2000 ident: 10.1016/j.bpj.2014.06.034_bib3 article-title: Regulation of contraction in striated muscle publication-title: Physiol. Rev. doi: 10.1152/physrev.2000.80.2.853 contributor: fullname: Gordon – volume: 100 start-page: 1005 year: 2011 ident: 10.1016/j.bpj.2014.06.034_bib7 article-title: Tropomyosin position on F-actin revealed by EM reconstruction and computational chemistry publication-title: Biophys. J. doi: 10.1016/j.bpj.2010.12.3697 contributor: fullname: Li – volume: 14 start-page: 33 year: 1996 ident: 10.1016/j.bpj.2014.06.034_bib14 article-title: VMD: visual molecular dynamics publication-title: J. Mol. Graph. doi: 10.1016/0263-7855(96)00018-5 contributor: fullname: Humphrey – volume: 22 start-page: 4978 year: 2013 ident: 10.1016/j.bpj.2014.06.034_bib21 article-title: Mutations in repeating structural motifs of tropomyosin cause gain of function in skeletal muscle myopathy patients publication-title: Hum. Mol. Genet. doi: 10.1093/hmg/ddt345 contributor: fullname: Marston – volume: 26 start-page: 1781 year: 2005 ident: 10.1016/j.bpj.2014.06.034_bib16 article-title: Scalable molecular dynamics with NAMD publication-title: J. Comput. Chem. doi: 10.1002/jcc.20289 contributor: fullname: Phillips – volume: 34 start-page: 285 year: 2013 ident: 10.1016/j.bpj.2014.06.034_bib20 article-title: α-Tropomyosin mutations in inherited cardiomyopathies publication-title: J. Muscle Res. Cell Motil. doi: 10.1007/s10974-013-9358-5 contributor: fullname: Redwood – volume: 545 start-page: 63 year: 2014 ident: 10.1016/j.bpj.2014.06.034_bib9 article-title: Tropomyosin movement on F-actin during muscle activation explained by energy landscapes publication-title: Arch. Biochem. Biophys. doi: 10.1016/j.abb.2014.01.001 contributor: fullname: Orzechowski – volume: 71 start-page: 121 year: 2005 ident: 10.1016/j.bpj.2014.06.034_bib1 article-title: Regulation of muscle contraction by tropomyosin and troponin: how structure illuminates function publication-title: Adv. Protein Chem. doi: 10.1016/S0065-3233(04)71004-9 contributor: fullname: Brown – volume: 364 start-page: 80 year: 2006 ident: 10.1016/j.bpj.2014.06.034_bib11 article-title: Solution NMR structure of the junction between tropomyosin molecules: implications for actin binding and regulation publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2006.08.033 contributor: fullname: Greenfield – volume: 552-553 start-page: 68 year: 2014 ident: 10.1016/j.bpj.2014.06.034_bib13 article-title: The structural dynamics of α-tropomyosin on F-actin shape the overlap complex between adjacent tropomyosin molecules publication-title: Arch. Biochem. Biophys. doi: 10.1016/j.abb.2013.09.011 contributor: fullname: Lehman – volume: 29 start-page: 213 year: 2008 ident: 10.1016/j.bpj.2014.06.034_bib2 article-title: Gestalt-binding of tropomyosin to actin filaments publication-title: J. Muscle Res. Cell Motil. doi: 10.1007/s10974-008-9157-6 contributor: fullname: Holmes – volume: 99 start-page: 862 year: 2010 ident: 10.1016/j.bpj.2014.06.034_bib18 article-title: Electron microscopy and persistence length analysis of semi-rigid smooth muscle tropomyosin strands publication-title: Biophys. J. doi: 10.1016/j.bpj.2010.05.004 contributor: fullname: Sousa – volume: 15 start-page: 333 year: 2005 ident: 10.1016/j.bpj.2014.06.034_bib4 article-title: Tropomyosin isoforms: divining rods for actin cytoskeleton function publication-title: Trends Cell Biol. doi: 10.1016/j.tcb.2005.04.007 contributor: fullname: Gunning – volume: 288 start-page: 9602 year: 2013 ident: 10.1016/j.bpj.2014.06.034_bib8 article-title: A periodic pattern of evolutionarily conserved basic and acidic residues constitutes the binding interface of actin-tropomyosin publication-title: J. Biol. Chem. doi: 10.1074/jbc.M113.451161 contributor: fullname: Barua |
SSID | ssj0012501 |
Score | 2.3980513 |
Snippet | Tropomyosin regulates a wide variety of actin filament functions and is best known for the role that it plays together with troponin in controlling muscle... |
SourceID | pubmedcentral proquest crossref pubmed elsevier |
SourceType | Open Access Repository Aggregation Database Index Database Publisher |
StartPage | 694 |
SubjectTerms | Actins - chemistry Actins - metabolism Amino Acid Sequence Atoms & subatomic particles Biochemistry Biophysics Molecular biology Molecular Dynamics Simulation Molecular Machines, Motors and Nanoscale Biophysics Molecular Sequence Data Mutation Protein Binding Protein Structure, Tertiary Proteins Tropomyosin - chemistry Tropomyosin - metabolism |
SummonAdditionalLinks | – databaseName: Open Access: Elsevier Open Archive Journals dbid: ABVKL link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3da9swED_alEFfxrp2m7u0aNCngahtybL8mIaFsm57ykbehGVLLKWTw5I-9L_vnT9C07E97NGWBNKddPc77gvgQiSlLpQreS2F4lSRjpPe4VbXSntfplXraP_6TV1_l58X2WIPpkMuDIVV9rK_k-mttO7_XPbUvFwtl5Tji-oV8T2aCCRyF_twQLXM8WofTK5-3HzZOhNQy_eN8xSnBYNzsw3zsqtbCvCSbRVPIf-mnv6En8-jKJ-opdkreNnjSTbptnwEey68hhddh8mHYxCTwCYbyjxm1PXsjjWeIeRjc2qO8OuhWS8Dm1L2FGsCm3HKcggnMJ99mk-ved8ngVeIfzZc17VP0irRMR60sKrKS5sXNs8LVSGgqaSsy6xGvWMzT9Vp8jK2tXPSOe1EocUbGIUmuHfA0FrUSnhdKuclYhGrVC3ypPJFGqfeFxF8HKhjVl01DDOEid0aJKUhUhoKlRMyAjnQz-yw1KC0_tey8UBr07-ntaHuRkkuVJFG8GE7jC-B3BtlcM19OycVSqPFHcHbjjXbTeIVQLsy1hHkO0zbTqAq27sjYfmzrbYtERFlcXz6f6d5D4f01YYMZmMYbX7fuzOEMRt73l_TRw_a7hU priority: 102 providerName: Elsevier |
Title | An Atomic Model of the Tropomyosin Cable on F-actin |
URI | https://dx.doi.org/10.1016/j.bpj.2014.06.034 https://www.ncbi.nlm.nih.gov/pubmed/25099808 https://www.proquest.com/docview/1553173692 https://search.proquest.com/docview/1552368837 https://pubmed.ncbi.nlm.nih.gov/PMC4129500 |
Volume | 107 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Na9wwEB2yKYVeQvrtJF1U6KmgrG3JsnzcLF3Sj5QetmVvxpIluiErL8nmkH-fkWwtTVt66FkySCPJb4Z5Mw_gHcsaWQnT0JYzQX1HOupxhyrZCmltk-uQaL_4Ks6_80_LYrkHRayFCaR9rVan7mp96lY_A7dys9aTyBObfLuYcQSpIk0nIxgh_MYQfUgdIKYPMnmCMnT_YyozkLrU5tLTuXjo2cm8KA9Ox4jDq0v-HZf-9Dt_p0_-gkfzQzgYHEky7Rf8FPaMewaPe2nJu-fApo5Mt77kmHi5syvSWYK-Hll4VYT1XXezcmTmy6ZI58ic-vIG9wIW8w-L2TkdBBKoRsdnS2Xb2izXmUxxz5USumxUWamyrIRGT0Zz3jZFi4CjCuvb0pRNqlpjuDHSsEqyl7DvOmdeA8EwUQpmZSOM5eiEKCFaVmbaVnmaW1sl8D5ap970bTDqyA-7rNGqtbdq7TlyjCfAo_3qAcd7fK7xN_2vz06irevhId3UXtYoK5mo8gTe7obxCfi8RuNMdxvm5ExIDLUTeNUfzW6R8XgTKB8c2m6Cb6_9cARvXWizPdyyo__-8hie-O0FumBxAvvb61vzBl2YrRrDo-nZj89fxjD6uDwbhwt8DwKU76I |
link.rule.ids | 230,314,727,780,784,885,3506,27569,27924,27925,45663,45874,53791,53793 |
linkProvider | National Library of Medicine |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwEB6VIkQviHcDbTESJySrSezYznFZdbWFtqdF2psVJ7bYCpwV3R7675nJY8WC4NBr7Ej22J75RjPzDcAHkVWmVL7ijRSKEyMdJ7vDnWmUCaHK6y7Qfnml5l_l52Wx3IPpWAtDaZWD7u91eqethy-ngzRP16sV1fiieUV8jy4CqdzlA3goC6OJQP98-WkbSkAbP7TNU5ymj6HNLsnLra8pvUt2HJ5C_ss4_Q0-_8yh_M0ozZ7CkwFNskm_4Gew5-NzeNT3l7x7AWIS2WRDdceMep59Z21gCPjYgloj_Lhrb1aRTal2irWRzTjVOMSXsJidLaZzPnRJ4DWinw03TROyvM5Mihstnap15XTptC5VjXCmlrKpigatjisCcdPoKnWN99J740VpxCvYj230h8DQVzRKBFMpHyQiEadUI3RWhzJP8xDKBD6O0rHrngvDjkli1xZFaUmUlhLlhExAjvKzOwdqUVf_77ejUdZ2eE03lnobZVqoMk_g_XYY3wEFN6ro29tuTi6UQX87gdf90WwXiVcAvcrUJKB3Dm07gTi2d0fi6lvHtS0RDxVp-uZ-u3kHj-eLywt7cX715S0c0EiXPFgcwf7m560_RkCzcSfdhf0FqPfv4A |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwEB6VViAuiDeBFozECcndJHYc57haWJVHqx4WqTcrfomtus6Kbg_994ydZNUC4tCzHckej_PNaD7PB_CBFa1shGup5UzQ2JGORtyhWlohvW9Lkwrtxyfi6Af_elad3ZD6SqR9o5eH4WJ1GJY_E7dyvTKTkSc2OT2ecQSpKs8na-sn92CvYuhkY6I-FBAQ2QexPEEZJgFjQTNRu_T6PJK6eOrcyaI0D07HvCNqTP4bnf6OPv8kUd5ApfljeDSEk2TaL_sJ7LjwFO73ApPXz4BNA5lu4sNjEkXPLkjnCUZ8ZBG1EVbX3eUykFl8PEW6QOY0PnIIz2Ex_7yYHdFBJoEaDH82VFrri9IUMsc9N1qYutV1o-u6EQbjGcO5bSuLsKMrH5vT1G2urXPcOelYI9kL2A1dcK-AYLIoBfOyFc5zDEW0EJbVhfFNmZfeNxl8HK2j1n0zDDWyxM4VWlVFq6rIlGM8Az7aTw1o3qO0wp_1_z7bH22thut0qaK4UVEz0ZQZvN8O40WI1Y02uO4qzSmZkJhwZ_CyP5rtIsfjzaC-dWjbCbHJ9u0R9L3UbHvwtdd3_vIdPDj9NFffv5x8ewMP404Tf7Dah93Nryt3gDHNRr9N3vsbKBjxcw |
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=An+Atomic+Model+of+the+Tropomyosin+Cable+on+F-actin&rft.jtitle=Biophysical+journal&rft.au=Orzechowski%2C+Marek&rft.au=Li%2C+Xiaochuan%C2%A0%28Edward%29&rft.au=Fischer%2C+Stefan&rft.au=Lehman%2C+William&rft.date=2014-08-05&rft.issn=0006-3495&rft.volume=107&rft.issue=3&rft.spage=694&rft.epage=699&rft_id=info:doi/10.1016%2Fj.bpj.2014.06.034&rft.externalDBID=n%2Fa&rft.externalDocID=10_1016_j_bpj_2014_06_034 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0006-3495&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0006-3495&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0006-3495&client=summon |