2010
DOI: 10.1073/pnas.1003604107
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The actin-myosin interface

Abstract: In order to understand the mechanism of muscle contraction at the atomic level, it is necessary to understand how myosin binds to actin in a reversible way. We have used a novel molecular dynamics technique constrained by an EM map of the actin-myosin complex at 13-Å resolution to obtain an atomic model of the strong-binding (rigor) actin-myosin interface. The constraining force resulting from the EM map during the molecular dynamics simulation was sufficient to convert the myosin head from the initial weak-bi… Show more

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Cited by 108 publications
(179 citation statements)
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References 27 publications
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“…When the first structure of myosin in a Rigorlike state was obtained (2), the structural basis for the long-known reciprocal nature of either strong actin or strong nucleotide binding became immediately evident (11). These insights have been confirmed with the highest-resolution actomyosin Rigor EM maps that have been published afterward (12,13). Strong binding to actin requires closure of the major cleft between the subdomains of the myosin motor to form a strong actin-binding interface, which in turn results in a relative movement of the subdomains of the myosin motor that contain the nucleotide-binding elements, Switch I and the P-loop.…”
supporting
confidence: 56%
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“…When the first structure of myosin in a Rigorlike state was obtained (2), the structural basis for the long-known reciprocal nature of either strong actin or strong nucleotide binding became immediately evident (11). These insights have been confirmed with the highest-resolution actomyosin Rigor EM maps that have been published afterward (12,13). Strong binding to actin requires closure of the major cleft between the subdomains of the myosin motor to form a strong actin-binding interface, which in turn results in a relative movement of the subdomains of the myosin motor that contain the nucleotide-binding elements, Switch I and the P-loop.…”
supporting
confidence: 56%
“…Here, the C-terminal basic residues of this loop seem to be in position to interact with D24, D25 of subdomain 1 of F-actin. The actin interface between myosin V and F-actin is otherwise quite similar to that described for myosin II bound to F-actin (12) and similar to that formed with the nucleotide-free myosin I bound to F-actin (13) (Fig. S5).…”
Section: Resultsmentioning
confidence: 48%
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“…1B shows the rigor-like crystal structure of myosin V (7), docked here to F actin based on electron microscopy reconstructions of decorated F actin (8). The two regions of the myosin head that contact actin belong, respectively, to the upper 50-kDa (henceforth "u50") domain and the central body.…”
mentioning
confidence: 99%