1vfq
From Proteopedia
(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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| - | [[Image:1vfq.gif|left|200px]]<br /> | + | [[Image:1vfq.gif|left|200px]]<br /><applet load="1vfq" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1vfq, resolution 1.9Å" /> | caption="1vfq, resolution 1.9Å" /> | ||
'''The Crystal Structure of Human Coactosin-like Protein at 1.9 A Resolution'''<br /> | '''The Crystal Structure of Human Coactosin-like Protein at 1.9 A Resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Human coactosin-like protein (CLP) shares high homology with coactosin, a | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1VFQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1VFQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VFQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: cytoskeleton]] | [[Category: cytoskeleton]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:34:47 2008'' |
Revision as of 13:34, 21 February 2008
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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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