2ifs
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(New page: 200px<br /><applet load="2ifs" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ifs" /> '''Structure of the N-WASP EVH1 domain in compl...)
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Revision as of 13:18, 23 January 2008
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Structure of the N-WASP EVH1 domain in complex with an extended WIP peptide
Overview
The WASP-interacting protein (WIP) targets WASP/WAVE proteins through a, constitutive interaction with an amino-terminal enabled/VASP homology, (EVH1) domain. Parallel investigations had previously identified two, distinct N-WASP binding motifs corresponding to WIP residues 451-461 and, 461-485, and we determined the structure of a complex between, WIP-(461-485) and the N-WASP EVH1 domain (Volkman, B. F., Prehoda, K. E., Scott, J. A., Peterson, F. C., and Lim, W. A. (2002) Cell 111, 565-576)., The present results show that, when combined, the WIP-(451-485) sequence, wraps further around the EVH1 domain, extending the interface observed, previously. Specific contacts with three WIP epitopes corresponded to, regions of high sequence conservation in the verprolin family. A central, polyproline motif occupied the canonical binding site but in a reversed, orientation relative to other EVH1 complexes. This interaction was, augmented in the amino- and carboxyl-terminal directions by additional, hydrophobic contacts involving WIP residues 454-459 and 475-478, respectively. Disruption of any of the three WIP epitopes reduced N-WASP, binding in cells, demonstrating a functional requirement for the entire, binding domain, which is significantly longer than the polyproline motifs, recognized by other EVH1 domains.
About this Structure
2IFS is a Single protein structure of sequence from Homo sapiens, rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Multiple WASP-interacting protein recognition motifs are required for a functional interaction with N-WASP., Peterson FC, Deng Q, Zettl M, Prehoda KE, Lim WA, Way M, Volkman BF, J Biol Chem. 2007 Mar 16;282(11):8446-53. Epub 2007 Jan 16. PMID:17229736
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