dc.contributor.author | Paul, DM | |
dc.contributor.author | Squire, JM | |
dc.contributor.author | Morris, EP | |
dc.date.accessioned | 2017-03-09T14:19:23Z | |
dc.date.issued | 2017-03-01 | |
dc.identifier.citation | Journal of structural biology, 2017, 197 (3), pp. 365 - 371 | |
dc.identifier.issn | 1047-8477 | |
dc.identifier.uri | https://repository.icr.ac.uk/handle/internal/479 | |
dc.identifier.eissn | 1095-8657 | |
dc.identifier.doi | 10.1016/j.jsb.2017.01.004 | |
dc.description.abstract | The structures of muscle thin filaments reconstituted using skeletal actin and cardiac troponin and tropomyosin have been determined with and without bound Ca2+ using electron microscopy and reference-free single particle analysis. The resulting density maps have been fitted with atomic models of actin, tropomyosin and troponin showing that: (i) the polarity of the troponin complex is consistent with our 2009 findings, with large shape changes in troponin between the two states; (ii) without Ca2+ the tropomyosin pseudo-repeats all lie at almost equivalent positions in the 'blocked' position on actin (over subdomains 1 and 2); (iii) in the active state the tropomyosin pseudo-repeats are all displaced towards subdomains 3 and 4 of actin, but the extent of displacement varies within the regulatory unit depending upon the axial location of the pseudo-repeats with respect to troponin. Individual pseudo-repeats with Ca2+ bound to troponin can be assigned either to the 'closed' state, a partly activated conformation, or the 'M-state', a fully activated conformation which has previously been thought to occur only when myosin heads bind. These results lead to a modified view of the steric blocking model of thin filament regulation in which cooperative activation is governed by troponin-mediated local interactions of the pseudo-repeats of tropomyosin with actin. | |
dc.format | Print-Electronic | |
dc.format.extent | 365 - 371 | |
dc.language | eng | |
dc.language.iso | eng | |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0 | |
dc.subject | Calcium | |
dc.subject | Actins | |
dc.subject | Tropomyosin | |
dc.subject | Troponin | |
dc.subject | Microscopy, Electron | |
dc.subject | Protein Binding | |
dc.subject | Actin Cytoskeleton | |
dc.title | Relaxed and active thin filament structures; a new structural basis for the regulatory mechanism. | |
dc.type | Journal Article | |
dcterms.dateAccepted | 2017-01-23 | |
rioxxterms.versionofrecord | 10.1016/j.jsb.2017.01.004 | |
rioxxterms.licenseref.uri | https://creativecommons.org/licenses/by/4.0 | |
rioxxterms.licenseref.startdate | 2017-03 | |
rioxxterms.type | Journal Article/Review | |
dc.relation.isPartOf | Journal of structural biology | |
pubs.issue | 3 | |
pubs.notes | Not known | |
pubs.organisational-group | /ICR | |
pubs.organisational-group | /ICR/Primary Group | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Structural Biology | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Structural Biology/Structural Electron Microscopy | |
pubs.organisational-group | /ICR | |
pubs.organisational-group | /ICR/Primary Group | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Structural Biology | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Structural Biology/Structural Electron Microscopy | |
pubs.publication-status | Published | |
pubs.volume | 197 | |
pubs.embargo.terms | Not known | |
icr.researchteam | Structural Electron Microscopy | |
dc.contributor.icrauthor | Morris, Edward | |