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  The actin-myosin interface

Lorenz, M., & Holmes, K. C. (2010). The actin-myosin interface. Proceedings of the National Academy of Sciences of the United States of America, 107(28), 12529-12534. doi:10.1073/pnas.1003604107.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-800C-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-800D-2
Genre: Journal Article
Alternative Title : The actin-myosin interface

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PNAS_107_2010_12529.pdf (Any fulltext), 3MB
 
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PNAS_107_2010_12529_Suppl.pdf (Supplementary material), 880KB
 
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 Creators:
Lorenz, Michael1, 2, Author              
Holmes, Kenneth C.1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497699              

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Free keywords: cryoelectron microscopy ; myosin II ; myosin V
 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−binding state to the strong−binding (rigor) state. Our actin−myosin model suggests extensive contacts between actin and the myosin head (S1). S1 binds to two actin monomers. The contact surface between actin and S1 has increased dramatically compared with previous models. A number of loops in S1 and actin are involved in establishing the interface. Our model also suggests how the loop carrying the critical Arg 405 Glu mutation in S1 found in a familial cardiomyopathy might be functionally involved

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Language(s): eng - English
 Dates: 2010-03-192010-04-302010-06-242010-07-13
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
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Publ. Info: National Academy of Sciences
Pages: - Volume / Issue: 107 (28) Sequence Number: - Start / End Page: 12529 - 12534 Identifier: ISSN: 0027-8424
CoNE: /journals/resource/954925427230