The structural basis of blebbistatin inhibition and specificity for myosin IIThe structural basis of blebbistatin inhibition and specificity for myosin II

Structural highlights

1yv3 is a 1 chain structure with sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MYS2_DICDI Myosin is a protein that binds to actin and has ATPase activity that is activated by actin.

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

The structural basis of blebbistatin inhibition and specificity for myosin II.,Allingham JS, Smith R, Rayment I Nat Struct Mol Biol. 2005 Apr;12(4):378-9. Epub 2005 Mar 6. PMID:15750603[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Allingham JS, Smith R, Rayment I. The structural basis of blebbistatin inhibition and specificity for myosin II. Nat Struct Mol Biol. 2005 Apr;12(4):378-9. Epub 2005 Mar 6. PMID:15750603 doi:10.1038/nsmb908

1yv3, resolution 2.00Å

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