1qqv
From Proteopedia
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[[Image:1qqv.gif|left|200px]] | [[Image:1qqv.gif|left|200px]] | ||
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'''SOLUTION STRUCTURE OF THE HEADPIECE DOMAIN OF CHICKEN VILLIN''' | '''SOLUTION STRUCTURE OF THE HEADPIECE DOMAIN OF CHICKEN VILLIN''' | ||
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[[Category: McKnight, C J.]] | [[Category: McKnight, C J.]] | ||
[[Category: Vardar, D.]] | [[Category: Vardar, D.]] | ||
| - | [[Category: | + | [[Category: F-actin binding domain]] |
| - | [[Category: | + | [[Category: Salt-bridge]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:36:11 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:36, 3 May 2008
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 Sat May 3 06:36:11 2008
