The determination of the 3D structure of myosin subfragment-1 provides a structural framework for understanding the molecular basis of cellular motility.
Provides structural basis for myosin motility research; leaves open translation to human cardiac therapeutics.
Directed movement is a characteristic of many living organisms and occurs as a result of the transformation of chemical energy into mechanical energy. Myosin is one of three families of molecular motors that are responsible for cellular motility. The three-dimensional structure of the head portion of myosin, or subfragment-1, which contains both the actin and nucleotide binding sites, is described. This structure of a molecular motor was determined by single crystal x-ray diffraction. The data provide a structural framework for understanding the molecular basis of motility.
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Rayment et al. (1993) studied this question.
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