2vge

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[[Image:2vge.jpg|left|200px]]<br /><applet load="2vge" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2vge, resolution 2.10&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE C-TERMINAL REGION OF HUMAN IASPP'''<br />
 
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==About this Structure==
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==Crystal structure of the C-terminal region of human iASPP==
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2VGE 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://oca.weizmann.ac.il/oca-bin/ocashort?id=2VGE OCA].
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<StructureSection load='2vge' size='340' side='right'caption='[[2vge]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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[[Category: Homo sapiens]]
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== Structural highlights ==
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[[Category: Single protein]]
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<table><tr><td colspan='2'>[[2vge]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VGE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VGE FirstGlance]. <br>
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[[Category: Jones, E Y.]]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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[[Category: Lu, X.]]
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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=2vge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vge OCA], [https://pdbe.org/2vge PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vge RCSB], [https://www.ebi.ac.uk/pdbsum/2vge PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vge ProSAT]</span></td></tr>
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[[Category: Robinson, R A.]]
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</table>
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[[Category: Siebold, C.]]
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== Function ==
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[[Category: alternative splicing]]
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[https://www.uniprot.org/uniprot/IASPP_HUMAN IASPP_HUMAN] Regulator that plays a central role in regulation of apoptosis and transcription via its interaction with NF-kappa-B and p53/TP53 proteins. Blocks transcription of HIV-1 virus by inhibiting the action of both NF-kappa-B and SP1. Also inhibits p53/TP53 function, possibly by preventing the association between p53/TP53 and ASPP1 or ASPP2, and therefore suppressing the subsequent activation of apoptosis.<ref>PMID:15489900</ref> <ref>PMID:10336463</ref> <ref>PMID:12134007</ref> <ref>PMID:12524540</ref>
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[[Category: ank repeat]]
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== Evolutionary Conservation ==
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[[Category: ankyrin repeats]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: apoptosis]]
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Check<jmol>
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[[Category: cytoplasm]]
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<jmolCheckbox>
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[[Category: iaspp]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vg/2vge_consurf.spt"</scriptWhenChecked>
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[[Category: nucleus]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: p53 binding protein]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: phosphorylation]]
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</jmolCheckbox>
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[[Category: repressor]]
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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=2vge ConSurf].
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[[Category: sh3 domain]]
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<div style="clear:both"></div>
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[[Category: transcription]]
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<div style="background-color:#fffaf0;">
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[[Category: transcription regulation]]
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== Publication Abstract from PubMed ==
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ASPP1 and ASPP2 are activators of p53-dependent apoptosis, whereas iASPP is an inhibitor of p53. Binding assays showed differential binding for C-terminal domains of iASPP and ASPP2 to the core domains of p53 family members p53, p63, and p73. We also determined a high-resolution crystal structure for the C terminus of iASPP, comprised of four ankyrin repeats and an SH3 domain. The crystal lattice revealed an interaction between eight sequential residues in one iASPP molecule and the p53-binding site of a neighboring molecule. ITC confirmed that a peptide corresponding to the crystallographic interaction shows specific binding to iASPP. The contributions of ankyrin repeat residues, in addition to those of the SH3 domain, generate distinctive architecture at the p53-binding site suitable for inhibition by small molecules. These results suggest that the binding properties of iASPP render it a target for antitumor therapeutics and provide a peptide-based template for compound design.
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:55:40 2008''
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Biochemical and structural studies of ASPP proteins reveal differential binding to p53, p63, and p73.,Robinson RA, Lu X, Jones EY, Siebold C Structure. 2008 Feb;16(2):259-68. PMID:18275817<ref>PMID:18275817</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 2vge" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Jones EY]]
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[[Category: Lu X]]
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[[Category: Robinson RA]]
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[[Category: Siebold C]]

Current revision

Crystal structure of the C-terminal region of human iASPP

PDB ID 2vge

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