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Structure of the actin-myosin complex and its implications for muscle contraction

MPG-Autoren
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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.
Protein Cristallography XDS, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Muscle Research, Max Planck Institute for Medical Research, Max Planck Society;

Externe Ressourcen

http://science.sciencemag.org/content/261/5117/58/tab-pdf
(beliebiger Volltext)

https://dx.doi.org/10.1126/science.8316858
(beliebiger Volltext)

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Zitation

Rayment, I., Holden, H. M., Whittaker, M., Yohn, C. B., Lorenz, M., Holmes, K. C., et al. (1993). Structure of the actin-myosin complex and its implications for muscle contraction. Science, 261(5117), 58-65. doi:10.1126/science.8316858.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0019-AA36-6
Zusammenfassung
Muscle contraction consists of a cyclical interaction between myosin and actin driven by the concomitant hydrolysis of adenosine triphosphate (ATP). A model for the rigor complex of F actin and the myosin head was obtained by combining the molecular structures of the individual proteins with the low-resolution electron density maps of the complex derived by cryo-electron microscopy and image analysis. The spatial relation between the ATP binding pocket on myosin and the major contact area on actin suggests a working hypothesis for the crossbridge cycle that is consistent with previous independent structural and biochemical studies.