1qqv: Difference between revisions
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qqv OCA], [http://www.ebi.ac.uk/pdbsum/1qqv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qqv RCSB]</span> | |||
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[[Category: salt-bridge]] | [[Category: salt-bridge]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:17:48 2008'' | ||
Revision as of 23:17, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF THE HEADPIECE DOMAIN OF CHICKEN VILLIN
OverviewOverview
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 StructureAbout this Structure
1QQV is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
ReferenceReference
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
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