1mke
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1mke" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mke" /> '''Structure of the N-WASP EVH1 Domain-WIP comp...)
Next diff →
Revision as of 19:21, 20 November 2007
|
Structure of the N-WASP EVH1 Domain-WIP complex
Overview
Missense mutants that cause the immune disorder Wiskott-Aldrich Syndrome, (WAS) map primarily to the Enabled/VASP homology 1 (EVH1) domain of the, actin regulatory protein WASP. This domain has been implicated in both, peptide and phospholipid binding. We show here that the N-WASP EVH1 domain, does not bind phosphatidyl inositol-(4,5)-bisphosphate, as previously, reported, but does specifically bind a 25 residue motif from the WASP, Interacting Protein (WIP). The NMR structure of the complex reveals a, novel recognition mechanism-the WIP ligand, which is far longer than, canonical EVH1 ligands, wraps around the domain, contacting a narrow but, extended surface. This recognition mechanism provides a basis for, understanding the effects of mutations that cause WAS.
About this Structure
1MKE is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Structure of the N-WASP EVH1 domain-WIP complex: insight into the molecular basis of Wiskott-Aldrich Syndrome., Volkman BF, Prehoda KE, Scott JA, Peterson FC, Lim WA, Cell. 2002 Nov 15;111(4):565-76. PMID:12437929 [[Category: ]]
Page seeded by OCA on Tue Nov 20 21:28:37 2007
