1qqv
From Proteopedia
(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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| - | [[Image:1qqv.gif|left|200px]]<br /><applet load="1qqv" size=" | + | [[Image:1qqv.gif|left|200px]]<br /><applet load="1qqv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qqv" /> | caption="1qqv" /> | ||
'''SOLUTION STRUCTURE OF THE HEADPIECE DOMAIN OF CHICKEN VILLIN'''<br /> | '''SOLUTION STRUCTURE OF THE HEADPIECE DOMAIN OF CHICKEN VILLIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A growing family of F-actin-bundling proteins harbors a modular | + | 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== | ==About this Structure== | ||
| - | 1QQV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http:// | + | 1QQV is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Buckley, D | + | [[Category: Buckley, D A.]] |
| - | [[Category: Frank, B | + | [[Category: Frank, B S.]] |
| - | [[Category: McKnight, C | + | [[Category: McKnight, C J.]] |
[[Category: Vardar, D.]] | [[Category: Vardar, D.]] | ||
[[Category: f-actin binding domain]] | [[Category: f-actin binding domain]] | ||
[[Category: salt-bridge]] | [[Category: salt-bridge]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:41 2008'' |
Revision as of 12:42, 21 February 2008
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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 Thu Feb 21 14:42:41 2008
