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==Structure of the N-WASP EVH1 domain in complex with an extended WIP peptide==
==Structure of the N-WASP EVH1 domain in complex with an extended WIP peptide==
<StructureSection load='2ifs' size='340' side='right'caption='[[2ifs]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2ifs' size='340' side='right'caption='[[2ifs]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ifs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IFS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2IFS FirstGlance]. <br>
<table><tr><td colspan='2'>[[2ifs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IFS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IFS FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">WASPIP, wasl ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2ifs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ifs OCA], [http://pdbe.org/2ifs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ifs RCSB], [http://www.ebi.ac.uk/pdbsum/2ifs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ifs ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ifs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ifs OCA], [https://pdbe.org/2ifs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ifs RCSB], [https://www.ebi.ac.uk/pdbsum/2ifs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ifs ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
[[http://www.uniprot.org/uniprot/WIPF1_HUMAN WIPF1_HUMAN]] Defects in WIPF1 are the cause of Wiskott-Aldrich syndrome type 2 (WAS2) [MIM:[http://omim.org/entry/614493 614493]]. WAS2 is an immunodeficiency disorder characterized by eczema, thrombocytopenia, recurrent infections, defective T-cell proliferation, and impaired natural killer cell function.<ref>PMID:22231303</ref> 
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/WIPF1_HUMAN WIPF1_HUMAN]] May have direct activity on the actin cytoskeleton. Induces actin polymerization and redistribution. Contributes with NCK1 and GRB2 in the recruitment and activation of WASL. May participate in regulating the subcellular localization of WASL, resulting in the disassembly of stress fibers in favor of filopodia formation (By similarity). Plays an important role in the intracellular motility of vaccinia virus by functioning as an adapter for recruiting WASL to vaccinia virus.<ref>PMID:9405671</ref> <ref>PMID:10878810</ref> 
[https://www.uniprot.org/uniprot/WASL_RAT WASL_RAT] Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Involved in various processes, such as mitosis and cytokinesis, via its role in the regulation of actin polymerization. Together with CDC42, involved in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. In addition to its role in the cytoplasm, also plays a role in the nucleus by regulating gene transcription, probably by promoting nuclear actin polymerization (By similarity). Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression. Plays a role in dendrite spine morphogenesis (By similarity).[UniProtKB:O00401][UniProtKB:Q91YD9]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ifs ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ifs ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:17229736</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ifs" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Wiskott-Aldrich syndrome protein|Wiskott-Aldrich syndrome protein]]
*[[Wiskott-Aldrich syndrome protein 3D structures|Wiskott-Aldrich syndrome protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Deng, Q]]
[[Category: Rattus norvegicus]]
[[Category: Peterson, F C]]
[[Category: Deng Q]]
[[Category: Volkman, B F]]
[[Category: Peterson FC]]
[[Category: Polyproline]]
[[Category: Volkman BF]]
[[Category: Protein-protein complex]]
[[Category: Signaling protein]]
[[Category: Verprolin]]
[[Category: Wiskott-aldrich syndrome]]

Latest revision as of 06:41, 1 May 2024

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

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