2ifs

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[[Image:2ifs.jpg|left|200px]]
 
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{{Structure
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==Structure of the N-WASP EVH1 domain in complex with an extended WIP peptide==
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|PDB= 2ifs |SIZE=350|CAPTION= <scene name='initialview01'>2ifs</scene>
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<StructureSection load='2ifs' size='340' side='right'caption='[[2ifs]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= WASPIP, wasl ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Homo sapiens, Rattus norvegicus])
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<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>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ifs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ifs OCA], [http://www.ebi.ac.uk/pdbsum/2ifs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ifs RCSB]</span>
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[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]
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/if/2ifs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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'''Structure of the N-WASP EVH1 domain in complex with an extended WIP peptide'''
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==See Also==
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*[[Wiskott-Aldrich syndrome protein 3D structures|Wiskott-Aldrich syndrome protein 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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==About this Structure==
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[[Category: Rattus norvegicus]]
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2IFS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens,_rattus_norvegicus Homo sapiens, rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IFS OCA].
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[[Category: Deng Q]]
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[[Category: Peterson FC]]
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==Reference==
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[[Category: Volkman BF]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17229736 17229736]
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[[Category: Homo sapiens, rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Deng, Q.]]
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[[Category: Peterson, F C.]]
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[[Category: Volkman, B F.]]
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[[Category: nmr]]
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[[Category: polyproline]]
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[[Category: protein-protein complex]]
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[[Category: verprolin]]
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[[Category: wiskott-aldrich syndrome]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:43:50 2008''
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Current revision

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

PDB ID 2ifs

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