This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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...) |
|||
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 13: | Line 13: | ||
[[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
|
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
