2IFS
Structure of the N-WASP EVH1 domain in complex with an extended WIP peptide
Summary for 2IFS
| Entry DOI | 10.2210/pdb2ifs/pdb |
| NMR Information | BMRB: 15020 |
| Descriptor | Wiskott-Aldrich Syndrome Protein interacting protein and Neural Wiskott-Aldrich syndrome protein chimera (1 entity in total) |
| Functional Keywords | wiskott-aldrich syndrome, verprolin, polyproline, protein-protein complex, signaling protein |
| Biological source | Homo sapiens, Rattus norvegicus (human, Norway rat) |
| Total number of polymer chains | 1 |
| Total formula weight | 19326.99 |
| Authors | Volkman, B.F.,Peterson, F.C.,Deng, Q. (deposition date: 2006-09-21, release date: 2007-01-16, Last modification date: 2024-05-01) |
| Primary citation | Peterson, F.C.,Deng, Q.,Zettl, M.,Prehoda, K.E.,Lim, W.A.,Way, M.,Volkman, B.F. Multiple WASP-interacting protein recognition motifs are required for a functional interaction with N-WASP. J.Biol.Chem., 282:8446-8453, 2007 Cited by PubMed Abstract: 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. PubMed: 17229736DOI: 10.1074/jbc.M609902200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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