Common structural motifs for the regulation of divergent class II myosins

J Biol Chem. 2010 May 28;285(22):16403-7. doi: 10.1074/jbc.R109.025551. Epub 2010 Mar 25.


This 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.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Amino Acid Motifs
  • Animals
  • Crystallography, X-Ray
  • Gene Expression Regulation
  • Humans
  • Models, Biological
  • Muscles / metabolism
  • Myosin Type II / chemistry*
  • Myosin Type II / metabolism*
  • Phosphorylation
  • Phylogeny
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Secondary
  • Protein Structure, Tertiary


  • Myosin Type II