2IFS

Structure of the N-WASP EVH1 domain in complex with an extended WIP peptide

2IFS の概要

• エントリーDOI: 10.2210/pdb2ifs/pdb
• NMR情報: BMRB: 15020
• 分子名称: Wiskott-Aldrich Syndrome Protein interacting protein and Neural Wiskott-Aldrich syndrome protein chimera (1 entity in total)
• 機能のキーワード: wiskott-aldrich syndrome, verprolin, polyproline, protein-protein complex, signaling protein
• 由来する生物種: Homo sapiens, Rattus norvegicus (human, Norway rat)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19326.99

構造登録者

Volkman, B.F.,Peterson, F.C.,Deng, Q. (登録日: 2006-09-21, 公開日: 2007-01-16, 最終更新日: 2024-05-01)

主引用文献

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

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: 17229736
DOI: 10.1074/jbc.M609902200

実験手法

SOLUTION NMR