1vfq
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(New page: 200px<br /> <applet load="1vfq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vfq, resolution 1.9Å" /> '''The Crystal Structur...)
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Revision as of 17:37, 12 November 2007
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The Crystal Structure of Human Coactosin-like Protein at 1.9 A Resolution
Contents |
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
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