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1qqv
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(New page: 200px<br /><applet load="1qqv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qqv" /> '''SOLUTION STRUCTURE OF THE HEADPIECE DOMAIN O...)
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Revision as of 22:47, 20 November 2007
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SOLUTION STRUCTURE OF THE HEADPIECE DOMAIN OF CHICKEN VILLIN
Overview
A growing family of F-actin-bundling proteins harbors a modular, F-actin-binding headpiece domain at the C terminus. Headpiece provides one, of the two F-actin-binding sites essential for filament bundling. Here, we, report the first structure of a functional headpiece domain. The NMR, structure of chicken villin headpiece (HP67) reveals two subdomains that, share a tightly packed hydrophobic core. The N-terminal subdomain contains, bends, turns, and a four-residue alpha-helix as well as a buried histidine, residue that imparts a pH-dependent folding. The C-terminal subdomain is, composed of three alpha-helices and its folding is pH-independent. Two, residues previously implicated in F-actin-binding form a buried, salt-bridge between the N and C-terminal subdomains. The rest of the, identified actin-binding residues are solvent-exposed and map onto a, unique F-actin-binding surface.
About this Structure
1QQV is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
NMR structure of an F-actin-binding "headpiece" motif from villin., Vardar D, Buckley DA, Frank BS, McKnight CJ, J Mol Biol. 1999 Dec 17;294(5):1299-310. PMID:10600386
Page seeded by OCA on Wed Nov 21 00:54:19 2007
