1t2l

From Proteopedia

Revision as of 14:55, 15 February 2008

Three Crystal Structures of Human Coactosin-like Protein

Overview

Human coactosin-like protein is an actin filament binding protein but does, not bind to globular actin. It associates with 5-Lipoxygenase both in vivo, and in vitro, playing important roles in modulating the activities of, actin and 5-Lipoxygenase. Coactosin counteracts the capping activity of, capping protein which inhibits the actin polymerization. We determined the, crystal structures of human coactosin-like protein by multi-wavelength, anomalous dispersion method. The structure showed a high level of, similarity to ADF-H domain, although their amino acid sequences share low, degree of homology. A few conserved hydrophobic residues that may, contribute to the folding were identified. This structure suggests, coactosin-like protein bind to F-actin in a different way from ADF/Cofilin, family. Combined with the information from previous mutagenesis studies, the binding sites for F-actin and 5-Lipoxygenase were analyzed, respectively. These two sites are quite close, which might prevent F-actin, and 5-Lipoxygenase from binding to coactosin simultaneously.

Disease

Known disease associated with this structure: Cardiomyopathy, dilated, 1M OMIM:[600824]

About this Structure

1T2L is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human coactosin-like protein., Liu L, Wei Z, Wang Y, Wan M, Cheng Z, Gong W, J Mol Biol. 2004 Nov 19;344(2):317-23. PMID:15522287

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