The structural basis of blebbistatin inhibition and specificity for myosin II

Nat Struct Mol Biol. 2005 Apr;12(4):378-9. doi: 10.1038/nsmb908. Epub 2005 Mar 6.


Molecular motors play a central role in cytoskeletal-mediated cellular processes and thus present an excellent target for cellular control by pharmacological agents. Yet very few such compounds have been found. We report here the structure of blebbistatin, which inhibits specific myosin isoforms, bound to the motor domain of Dictyostelium discoideum myosin II. This reveals the structural basis for its specificity and provides insight into the development of new agents.

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

  • Animals
  • Binding Sites
  • Dictyostelium / chemistry
  • Dictyostelium / metabolism
  • Heterocyclic Compounds, 4 or More Rings / chemistry*
  • Heterocyclic Compounds, 4 or More Rings / pharmacology*
  • Models, Molecular
  • Myosin Type II / antagonists & inhibitors*
  • Myosin Type II / chemistry*
  • Myosin Type II / metabolism
  • Protein Isoforms / chemistry
  • Protein Isoforms / metabolism
  • Protein Structure, Tertiary
  • Substrate Specificity


  • Heterocyclic Compounds, 4 or More Rings
  • Protein Isoforms
  • blebbistatin
  • Myosin Type II