1tr2

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[[Image:1tr2.gif|left|200px]]
[[Image:1tr2.gif|left|200px]]
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{{Structure
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|PDB= 1tr2 |SIZE=350|CAPTION= <scene name='initialview01'>1tr2</scene>, resolution 2.90&Aring;
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The line below this paragraph, containing "STRUCTURE_1tr2", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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|GENE= VCL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_1tr2| PDB=1tr2 | SCENE= }}
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|RELATEDENTRY=[[1rke|1RKE]], [[1rkc|1RKC]], [[1ydi|1YDI]], [[1syq|1SYQ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tr2 OCA], [http://www.ebi.ac.uk/pdbsum/1tr2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tr2 RCSB]</span>
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'''Crystal structure of human full-length vinculin (residues 1-1066)'''
'''Crystal structure of human full-length vinculin (residues 1-1066)'''
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[[Category: Izard, T.]]
[[Category: Izard, T.]]
[[Category: Vonrhein, C.]]
[[Category: Vonrhein, C.]]
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[[Category: actin-binding]]
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[[Category: Actin-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:16:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:59:55 2008''
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Revision as of 07:16, 3 May 2008

Image:1tr2.gif

Template:STRUCTURE 1tr2

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 Page seeded by OCA on Sat May 3 10:16:33 2008

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OCA

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