2uwq

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(New page: 200px<br /> <applet load="2uwq" size="450" color="white" frame="true" align="right" spinBox="true" caption="2uwq" /> '''SOLUTION STRUCTURE OF ASPP2 N-TERMINUS'''<b...)
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[[Image:2uwq.gif|left|200px]]<br />
 
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<applet load="2uwq" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2uwq" />
 
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'''SOLUTION STRUCTURE OF ASPP2 N-TERMINUS'''<br />
 
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==Overview==
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==Solution structure of ASPP2 N-terminus==
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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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<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 [https://en.wikipedia.org/wiki/Human Human]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2UWQ FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ycs|1ycs]]</div></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=2uwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uwq OCA], [https://pdbe.org/2uwq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uwq RCSB], [https://www.ebi.ac.uk/pdbsum/2uwq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uwq ProSAT]</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/main_output.php?pdb_ID=2uwq 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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==About this Structure==
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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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2UWQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2UWQ OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17594908 17594908]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 2uwq" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Andreeva, A.]]
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<references/>
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[[Category: Fersht, A.R.]]
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__TOC__
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[[Category: Rutherford, T.J.]]
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</StructureSection>
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[[Category: Tidow, H.]]
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[[Category: Human]]
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[[Category: ank repeat]]
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[[Category: Large Structures]]
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[[Category: apoptosis]]
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[[Category: Andreeva, A]]
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[[Category: aspp2]]
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[[Category: Fersht, A R]]
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[[Category: cell cycle]]
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[[Category: Rutherford, T J]]
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[[Category: sh3-binding]]
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[[Category: Tidow, H]]
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[[Category: sh3-domain]]
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[[Category: Ank repeat]]
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[[Category: ubiquitin-like]]
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[[Category: Apoptosis]]
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[[Category: Aspp2]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:40:07 2007''
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[[Category: Cell cycle]]
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[[Category: Sh3-binding]]
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[[Category: Sh3-domain]]
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[[Category: Ubiquitin-like]]

Current revision

Solution structure of ASPP2 N-terminus

PDB ID 2uwq

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