Key result
A structural model for the rigor complex of F actin and the myosin head suggests a working hypothesis for the crossbridge cycle driven by ATP hydrolysis.
Provides a structural model of the actin-myosin complex that explains the crossbridge cycle of muscle contraction.
Extends structural models of contraction; leaves open clinical relevance for human cardiac muscle.
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.
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Rayment et al. (1993) studied Muscle contraction. A structural model for the rigor complex of F actin and the myosin head suggests a working hypothesis for the crossbridge cycle driven by ATP hydrolysis.
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