2ifs
From Proteopedia
(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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==Overview== | ==Overview== | ||
| - | The WASP-interacting protein (WIP) targets WASP/WAVE proteins through a | + | 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== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Deng, Q.]] | [[Category: Deng, Q.]] | ||
| - | [[Category: Peterson, F | + | [[Category: Peterson, F C.]] |
| - | [[Category: Volkman, B | + | [[Category: Volkman, B F.]] |
[[Category: nmr]] | [[Category: nmr]] | ||
[[Category: polyproline]] | [[Category: polyproline]] | ||
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[[Category: wiskott-aldrich syndrome]] | [[Category: wiskott-aldrich syndrome]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:52:11 2008'' |
Revision as of 15:52, 21 February 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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