Abstract
An atomic model for the rigor complex of F-actin and the myosin head has been obtained by combining the molecular structures of the individual proteins (Rayment et al. 1993a) (Holmes et al. 1990) (Lorenz et al. 1993) with the low resolution electron density maps of the actomyosin complex derived by cryoelectron microscopy (Rayment et al. 1993b) (Schröder et al. 1993). A model for the actomyosin interaction has been proposed in which the actin binding sites and nucleotide binding sites of SI are functionally linked by a cleft in the 50K domain of SI which is thought to close on binding to F-actin (Rayment et al. 1993b). The closing of the cleft is likely to be an essential part of the weak/strong sequence of the actomyosin interaction. The initial actomyosin interaction probably involves only part of the surface, the full rigor complex develops on closure of the cleft. The obligatory sequencestereo specific-weak/strong prevents the cross-bridge from binding unstrained in the strong state. Tropomyosin in the “off” state appears to inhibit the closing of the cleft.
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Holmes, K.C. (1995). The Actomyosin Interaction. In: Jockusch, B.M., Mandelkow, E., Weber, K. (eds) The Cytoskeleton. Colloquium der Gesellschaft für Biologische Chemie 14.–16. April 1994 in Mosbach/Baden, vol 45. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-79482-7_4
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DOI: https://doi.org/10.1007/978-3-642-79482-7_4
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