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J Mol Biol. 2011 Oct 14;413(1):97-105. doi: 10.1016/j.jmb.2011.08.039. Epub 2011 Aug 22.

The interaction of cofilin with the actin filament.

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1
Department of Biomedical Engineering, Washington University in St. Louis, St. Louis, MO 63130, USA.

Abstract

Cofilin is a key actin-binding protein that is critical for controlling the assembly of actin within the cell. Here, we present the results of molecular docking and dynamics studies using a muscle actin filament and human cofilin I. Guided by extensive mutagenesis results and other biophysical and structural studies, we arrive at a model for cofilin bound to the actin filament. This predicted structure agrees very well with electron microscopy results for cofilin-decorated filaments, provides molecular insight into how the known F- and G-actin sites on cofilin interact with the filament, and also suggests new interaction sites that may play a role in cofilin binding. The resulting atomic-scale model also helps us understand the molecular function and regulation of cofilin and provides testable data for future experimental and simulation work.

PMID:
21875597
PMCID:
PMC3184344
DOI:
10.1016/j.jmb.2011.08.039
[Indexed for MEDLINE]
Free PMC Article
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