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Journal Article

The actin-myosin interface

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Lorenz,  Michael
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society;

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Holmes,  Kenneth C.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002E-800C-4
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