1tr2
From Proteopedia
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Crystal structure of human full-length vinculin (residues 1-1066)
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.
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 Mon Nov 12 19:27:07 2007
