1qkr
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(New page: 200px<br /><applet load="1qkr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qkr, resolution 1.8Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 22:39, 20 November 2007
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CRYSTAL STRUCTURE OF THE VINCULIN TAIL AND A PATHWAY FOR ACTIVATION
Overview
Vinculin plays a dynamic role in the assembly of the actin cytoskeleton. A, strong interaction between its head and tail domains that regulates, binding to other cytoskeletal components is disrupted by acidic, phospholipids. Here, we present the crystal structure of the vinculin, tail, residues 879-1066. Five amphipathic helices form an antiparallel, bundle that resembles exchangeable apolipoproteins. A C-terminal arm wraps, across the base of the bundle and emerges as a hydrophobic hairpin, surrounded by a collar of basic residues, adjacent to the N terminus. We, show that the C-terminal arm is required for binding to acidic, phospholipids but not to actin, and that binding either ligand induces, conformational changes that may represent the first step in activation.
About this Structure
1QKR is a Single protein structure of sequence from Gallus gallus with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the vinculin tail suggests a pathway for activation., Bakolitsa C, de Pereda JM, Bagshaw CR, Critchley DR, Liddington RC, Cell. 1999 Dec 10;99(6):603-13. PMID:10612396
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