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2uwq
From Proteopedia
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| - | [[Image:2uwq.jpg|left|200px]] | ||
| - | + | ==Solution structure of ASPP2 N-terminus== | |
| - | + | <StructureSection load='2uwq' size='340' side='right'caption='[[2uwq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <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> | |
| - | + | </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> | |
| - | | | + | <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> |
| - | + | </table> | |
| - | | | + | == Evolutionary Conservation == |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | + | Check<jmol> | |
| - | + | <jmolCheckbox> | |
| - | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uw/2uwq_consurf.spt"</scriptWhenChecked> | |
| - | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |
| - | + | <text>to colour the structure by Evolutionary Conservation</text> | |
| - | == | + | </jmolCheckbox> |
| + | </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]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
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. | 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. | ||
| - | + | 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-terminal domain (N-ASPP2) reveals a ubiquitin-like fold., Tidow H, Andreeva A, Rutherford TJ, Fersht AR | + | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2uwq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Andreeva, A]] | ||
| + | [[Category: Fersht, A R]] | ||
| + | [[Category: Rutherford, T J]] | ||
| + | [[Category: Tidow, H]] | ||
| + | [[Category: Ank repeat]] | ||
| + | [[Category: Apoptosis]] | ||
| + | [[Category: Aspp2]] | ||
| + | [[Category: Cell cycle]] | ||
| + | [[Category: Sh3-binding]] | ||
| + | [[Category: Sh3-domain]] | ||
| + | [[Category: Ubiquitin-like]] | ||
Current revision
Solution structure of ASPP2 N-terminus
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Categories: Human | Large Structures | Andreeva, A | Fersht, A R | Rutherford, T J | Tidow, H | Ank repeat | Apoptosis | Aspp2 | Cell cycle | Sh3-binding | Sh3-domain | Ubiquitin-like

