1YV3

The structural basis of blebbistatin inhibition and specificity for myosin II

Summary for 1YV3

• Entry DOI: 10.2210/pdb1yv3/pdb
• Related: 1VOM
• Descriptor: Myosin II heavy chain, MAGNESIUM ION, VANADATE ION, ... (7 entities in total)
• Functional Keywords: myosin, blebbistatin, myosin ii inhibitor, myosin-inhibitor complex, metastable state, contractile protein
• Biological source: Dictyostelium discoideum
• Cellular location: Cytoplasm, cell cortex: P08799
• Total number of polymer chains: 1
• Total formula weight: 87692.26

Authors

Allingham, J.S.,Smith, R.,Rayment, I. (deposition date: 2005-02-14, release date: 2005-03-08, Last modification date: 2023-08-23)

Primary citation

Allingham, J.S.,Smith, R.,Rayment, I.
The structural basis of blebbistatin inhibition and specificity for myosin II.
Nat.Struct.Mol.Biol., 12:378-379, 2005

PubMed Abstract: 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.

PubMed: 15750603
DOI: 10.1038/nsmb908

Experimental method

X-RAY DIFFRACTION (2 Å)