1vfq | pdb_00001vfq
The Crystal Structure of Human Coactosin-like Protein at 1.9 A Resolution
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| 1vfq, resolution 1.9Å | |||||||||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
Human coactosin-like protein (CLP) shares high homology with coactosin, a filamentous (F)-actin binding protein, and interacts with 5LO and F-actin. As a tumor antigen, CLP is overexpressed in tumor tissue cells or cell lines, and the encoded epitopes can be recognized by cellular and humoral immune systems. To gain a better understanding of its various functions and interactions with related proteins, the crystal structure of CLP expressed in Escherichia coli has been determined to 1.9 A resolution. The structure features a central beta-sheet surrounded by helices, with two very tight hydrophobic cores on each side of the sheet. CLP belongs to the actin depolymerizing protein superfamily, and is similar to yeast cofilin and actophilin. Based on our structural analysis, we observed that CLP forms a polymer along the crystallographic b axis with the exact same repeat distance as F-actin. A model for the CLP polymer and F-actin binding has therefore been proposed.
Disease
Known disease associated with this structure: Cardiomyopathy, dilated, 1M OMIM:[600824]
About this Structure
1VFQ 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 at 1.9 A resolution., Li X, Liu X, Lou Z, Duan X, Wu H, Liu Y, Rao Z, Protein Sci. 2004 Nov;13(11):2845-51. Epub 2004 Sep 30. PMID:15459340
Page seeded by OCA on Thu Mar 20 14:44:56 2008
