1mke

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{{Seed}}
 
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[[Image:1mke.png|left|200px]]
 
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==Structure of the N-WASP EVH1 Domain-WIP complex==
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The line below this paragraph, containing "STRUCTURE_1mke", creates the "Structure Box" on the page.
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<StructureSection load='1mke' size='340' side='right'caption='[[1mke]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1mke]] 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=1MKE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MKE FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mke OCA], [https://pdbe.org/1mke PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mke RCSB], [https://www.ebi.ac.uk/pdbsum/1mke PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mke ProSAT]</span></td></tr>
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{{STRUCTURE_1mke| PDB=1mke | SCENE= }}
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</table>
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== Function ==
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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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== 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/mk/1mke_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=1mke ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Missense mutants that cause the immune disorder Wiskott-Aldrich Syndrome (WAS) map primarily to the Enabled/VASP homology 1 (EVH1) domain of the actin regulatory protein WASP. This domain has been implicated in both peptide and phospholipid binding. We show here that the N-WASP EVH1 domain does not bind phosphatidyl inositol-(4,5)-bisphosphate, as previously reported, but does specifically bind a 25 residue motif from the WASP Interacting Protein (WIP). The NMR structure of the complex reveals a novel recognition mechanism-the WIP ligand, which is far longer than canonical EVH1 ligands, wraps around the domain, contacting a narrow but extended surface. This recognition mechanism provides a basis for understanding the effects of mutations that cause WAS.
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===Structure of the N-WASP EVH1 Domain-WIP complex===
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Structure of the N-WASP EVH1 domain-WIP complex: insight into the molecular basis of Wiskott-Aldrich Syndrome.,Volkman BF, Prehoda KE, Scott JA, Peterson FC, Lim WA Cell. 2002 Nov 15;111(4):565-76. PMID:12437929<ref>PMID:12437929</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1mke" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12437929}}, adds the Publication Abstract to the page
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*[[Wiskott-Aldrich syndrome protein 3D structures|Wiskott-Aldrich syndrome protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12437929 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12437929}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Homo sapiens]]
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1MKE is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKE OCA].
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[[Category: Large Structures]]
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[[Category: Rattus norvegicus]]
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==Reference==
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[[Category: Lim WA]]
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<ref group="xtra">PMID:12437929</ref><references group="xtra"/>
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[[Category: Peterson FC]]
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[[Category: Lim, W A.]]
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[[Category: Prehoda KE]]
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[[Category: Peterson, F C.]]
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[[Category: Scott JA]]
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[[Category: Prehoda, K E.]]
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[[Category: Volkman BF]]
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[[Category: Scott, J A.]]
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 07:05:57 2009''
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Current revision

Structure of the N-WASP EVH1 Domain-WIP complex

PDB ID 1mke

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