1t2l

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spinqualitylabelsall models PDB ID 1t2l Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.8Å
Coordinates:	save as pdb, mmCIF, xml

Three Crystal Structures of Human Coactosin-like Protein

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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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