1qqv: Difference between revisions
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[[Image:1qqv.gif|left|200px]] | [[Image:1qqv.gif|left|200px]] | ||
'''SOLUTION STRUCTURE OF THE HEADPIECE DOMAIN OF CHICKEN VILLIN''' | {{Structure | ||
|PDB= 1qqv |SIZE=350|CAPTION= <scene name='initialview01'>1qqv</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
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'''SOLUTION STRUCTURE OF THE HEADPIECE DOMAIN OF CHICKEN VILLIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1QQV is a [ | 1QQV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QQV OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10600386 10600386] | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: salt-bridge]] | [[Category: salt-bridge]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:41:29 2008'' | ||
Revision as of 14:41, 20 March 2008
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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
Page seeded by OCA on Thu Mar 20 13:41:29 2008