2pbd: Difference between revisions

Revision as of 07:38, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2pbd.png

Template:STRUCTURE 2pbd

Ternary complex of profilin-actin with the poly-PRO-GAB domain of VASPTernary complex of profilin-actin with the poly-PRO-GAB domain of VASP

Template:ABSTRACT PUBMED 17914456

About this StructureAbout this Structure

2PBD is a Protein complex structure of sequences from Homo sapiens and Oryctolagus cuniculus. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP., Ferron F, Rebowski G, Lee SH, Dominguez R, EMBO J. 2007 Oct 31;26(21):4597-606. Epub 2007 Oct 4. PMID:17914456

Page seeded by OCA on Mon Jul 28 07:38:28 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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+{{Seed}}
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 {{STRUCTURE_2pbd|  PDB=2pbd  |  SCENE=  }}
-'''Ternary complex of profilin-actin with the poly-PRO-GAB domain of VASP*'''
+===Ternary complex of profilin-actin with the poly-PRO-GAB domain of VASP*===
-==Overview==
+<!--
-Cells sustain high rates of actin filament elongation by maintaining a large pool of actin monomers above the critical concentration for polymerization. Profilin-actin complexes constitute the largest fraction of polymerization-competent actin monomers. Filament elongation factors such as Ena/VASP and formin catalyze the transition of profilin-actin from the cellular pool onto the barbed end of growing filaments. The molecular bases of this process are poorly understood. Here we present structural and energetic evidence for two consecutive steps of the elongation mechanism: the recruitment of profilin-actin by the last poly-Pro segment of vasodilator-stimulated phosphoprotein (VASP) and the binding of profilin-actin simultaneously to this poly-Pro and to the G-actin-binding (GAB) domain of VASP. The actin monomer bound at the GAB domain is proposed to be in position to join the barbed end of the growing filament concurrently with the release of profilin.
+The line below this paragraph, {{ABSTRACT_PUBMED_17914456}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17914456 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17914456}}
 ==About this Structure==
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 [[Category: Ternary complex]]
 [[Category: Vasp]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 12:46:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:38:28 2008''