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2uwq

From Proteopedia

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[[Image:2uwq.png|left|200px]]
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==SOLUTION STRUCTURE OF ASPP2 N-TERMINUS==
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<StructureSection load='2uwq' size='340' side='right' caption='[[2uwq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2uwq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UWQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2UWQ FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ycs|1ycs]]</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2uwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uwq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2uwq RCSB], [http://www.ebi.ac.uk/pdbsum/2uwq PDBsum]</span></td></tr>
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<table>
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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/uw/2uwq_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/chain_selection.php?pdb_ID=2ata 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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Proteins of the ASPP family bind to p53 and regulate p53-mediated apoptosis. Two family members, ASPP1 and ASPP2, have pro-apoptotic functions while iASPP shows anti-apoptotic responses. However, both the mechanism of enhancement/repression of apoptosis and the molecular basis for their different responses remain unknown. To address the role of the N-termini of pro-apoptotic ASPP proteins, we solved the solution structure of N-ASPP2 (1-83) by NMR spectroscopy. The structure of this domain reveals a beta-Grasp ubiquitin-like fold. Our findings suggest a possible role for the N-termini of ASPP proteins in binding to other proteins in the apoptotic response network and thus mediating their selective pro-apoptotic function.
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{{STRUCTURE_2uwq| PDB=2uwq | SCENE= }}
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Solution structure of ASPP2 N-terminal domain (N-ASPP2) reveals a ubiquitin-like fold.,Tidow H, Andreeva A, Rutherford TJ, Fersht AR J Mol Biol. 2007 Aug 24;371(4):948-58. Epub 2007 May 13. PMID:17594908<ref>PMID:17594908</ref>
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===SOLUTION STRUCTURE OF ASPP2 N-TERMINUS===
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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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{{ABSTRACT_PUBMED_17594908}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2uwq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UWQ OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:017594908</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Andreeva, A.]]
[[Category: Andreeva, A.]]

Revision as of 02:11, 1 October 2014

SOLUTION STRUCTURE OF ASPP2 N-TERMINUS

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