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Common structural motifs for the regulation of divergent class II myosins Lowey S; Trybus KMJ Biol Chem 2010[May]; 285 (22): 16403-7This minireview focuses on structural studies that have provided insights into our current understanding of thick filament regulation in muscle. We describe how different domains in the myosin molecule interact to produce an inactive "off" state; included are head-head and head-rod interactions, the role of the regulatory light chain, and the significance of the alpha-helical coiled-coil rod in regulation. Several of these interactions have now been visualized in a wide variety of native myosin filaments, testifying to the generality of these structural motifs across the phylogenetic tree.|Amino Acid Motifs[MESH]|Animals[MESH]|Crystallography, X-Ray[MESH]|Gene Expression Regulation[MESH]|Humans[MESH]|Models, Biological[MESH]|Muscles/metabolism[MESH]|Myosin Type II/*chemistry/*metabolism[MESH]|Phosphorylation[MESH]|Phylogeny[MESH]|Protein Binding[MESH]|Protein Conformation[MESH]|Protein Structure, Secondary[MESH]|Protein Structure, Tertiary[MESH] |
