The structural basis of blebbistatin inhibition and specificity for myosin II
- 6 March 2005
- journal article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 12 (4), 378-379
- https://doi.org/10.1038/nsmb908
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.Keywords
This publication has 15 references indexed in Scilit:
- Adhesion-contractile balance in myocyte differentiationJournal of Cell Science, 2004
- Kinetic Mechanism of Blebbistatin Inhibition of Nonmuscle Myosin IIBBiochemistry, 2004
- Two Distinct Actin Networks Drive the Protrusion of Migrating CellsScience, 2004
- Mechanism of Blebbistatin Inhibition of Myosin IIJournal of Biological Chemistry, 2004
- Specificity of blebbistatin, an inhibitor of myosin IIJournal of Muscle Research and Cell Motility, 2004
- Biochemical and molecular characterization of diseases linked to motor proteinsTrends in Biochemical Sciences, 2003
- Mechanism of Inhibition of Skeletal Muscle Actomyosin by N-Benzyl-p-toluenesulfonamideBiochemistry, 2003
- Dissecting Temporal and Spatial Control of Cytokinesis with a Myosin II InhibitorScience, 2003
- A small-molecule inhibitor of skeletal muscle myosin IINature Cell Biology, 2001
- A Millennial Myosin CensusMolecular Biology of the Cell, 2001