Structure of the regulatory domain of scallop myosin at 2.8 A resolution

Nature. 1994 Mar 24;368(6469):306-12. doi: 10.1038/368306a0.


The regulatory domain of scallop myosin is a three-chain protein complex that switches on this motor in response to Ca2+ binding. This domain has been crystallized and the structure solved to 2.8 A resolution. Side-chain interactions link the two light chains in tandem to adjacent segments of the heavy chain bearing the IQ-sequence motif. The Ca(2+)-binding site is a novel EF-hand motif on the essential light chain and is stabilized by linkages involving the heavy chain and both light chains, accounting for the requirement of all three chains for Ca2+ binding and regulation in the intact myosin molecule.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Calcium / metabolism
  • Computer Graphics
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Mollusca
  • Myosins / chemistry*
  • Myosins / metabolism
  • Myosins / physiology
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Protein Conformation


  • Peptide Fragments
  • Myosins
  • Calcium