1tr2
From Proteopedia
(New page: 200px<br /> <applet load="1tr2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tr2, resolution 2.90Å" /> '''Crystal structure o...) |
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| - | [[Image:1tr2.gif|left|200px]]<br /> | + | [[Image:1tr2.gif|left|200px]]<br /><applet load="1tr2" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1tr2, resolution 2.90Å" /> | caption="1tr2, resolution 2.90Å" /> | ||
'''Crystal structure of human full-length vinculin (residues 1-1066)'''<br /> | '''Crystal structure of human full-length vinculin (residues 1-1066)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Alterations in the actin cytoskeleton following the formation of | + | Alterations in the actin cytoskeleton following the formation of cell-matrix and cell-cell junctions are orchestrated by vinculin. Vinculin associates with a large number of cytoskeletal and signaling proteins, and this flexibility is thought to contribute to rapid dissociation and reassociations of adhesion complexes. Intramolecular interactions between vinculin's head (Vh) and tail (Vt) domains limit access of its binding sites for other adhesion proteins. While the crystal structures of the Vh and Vt domains are known, these domains represent less than half of the entire protein and are separated by a large central region of unknown structure and function. Here we report the crystal structure of human full-length vinculin to 2.85 A resolution. In its resting state, vinculin is a loosely packed collection of alpha-helical bundles held together by Vh-Vt interactions. The three new well ordered alpha-helical bundle domains are similar in their structure to either Vh (Vh2 and Vh3) or to Vt (Vt2) and their loose packing provides the necessary flexibility that allows vinculin to interact with its various protein partners at sites of cell adhesion. |
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| + | ==Disease== | ||
| + | Known disease associated with this structure: Cardiomyopathy, dilated, 1W OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=193065 193065]] | ||
==About this Structure== | ==About this Structure== | ||
| - | 1TR2 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:// | + | 1TR2 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=1TR2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bois, P | + | [[Category: Bois, P R.]] |
| - | [[Category: Borgon, R | + | [[Category: Borgon, R A.]] |
[[Category: Bricogne, G.]] | [[Category: Bricogne, G.]] | ||
[[Category: Izard, T.]] | [[Category: Izard, T.]] | ||
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[[Category: actin-binding]] | [[Category: actin-binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:16:29 2008'' |
Revision as of 13:16, 21 February 2008
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Crystal structure of human full-length vinculin (residues 1-1066)
Contents |
Overview
Alterations in the actin cytoskeleton following the formation of cell-matrix and cell-cell junctions are orchestrated by vinculin. Vinculin associates with a large number of cytoskeletal and signaling proteins, and this flexibility is thought to contribute to rapid dissociation and reassociations of adhesion complexes. Intramolecular interactions between vinculin's head (Vh) and tail (Vt) domains limit access of its binding sites for other adhesion proteins. While the crystal structures of the Vh and Vt domains are known, these domains represent less than half of the entire protein and are separated by a large central region of unknown structure and function. Here we report the crystal structure of human full-length vinculin to 2.85 A resolution. In its resting state, vinculin is a loosely packed collection of alpha-helical bundles held together by Vh-Vt interactions. The three new well ordered alpha-helical bundle domains are similar in their structure to either Vh (Vh2 and Vh3) or to Vt (Vt2) and their loose packing provides the necessary flexibility that allows vinculin to interact with its various protein partners at sites of cell adhesion.
Disease
Known disease associated with this structure: Cardiomyopathy, dilated, 1W OMIM:[193065]
About this Structure
1TR2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human vinculin., Borgon RA, Vonrhein C, Bricogne G, Bois PR, Izard T, Structure. 2004 Jul;12(7):1189-97. Epub 2004 Jun 3. PMID:15242595
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