2pav
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(New page: 200px<br /> <applet load="2pav" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pav, resolution 1.800Å" /> '''Ternary complex of...)
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Revision as of 21:15, 12 November 2007
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Ternary complex of Profilin-Actin with the Last Poly-Pro of Human 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.
About this Structure
2PAV is a Protein complex structure of sequences from Homo sapiens and Oryctolagus cuniculus with CA and ATP as ligands. Full crystallographic information is available from OCA.
Reference
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 4;. PMID:17914456
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