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4eoz

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'''Unreleased structure'''
 
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The entry 4eoz is ON HOLD
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==Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal domain==
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<StructureSection load='4eoz' size='340' side='right'caption='[[4eoz]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4eoz]] is a 4 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=4EOZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EOZ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4eoz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eoz OCA], [https://pdbe.org/4eoz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eoz RCSB], [https://www.ebi.ac.uk/pdbsum/4eoz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eoz ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/SPOP_HUMAN SPOP_HUMAN]] Inhibits IPF1/PDX1 transactivation of established target promoters, such as insulin, may be by recruiting a repressor complex (By similarity). In complex with CUL3, involved in ubiquitination of BMI1, H2AFY and DAXX, and probably also in ubiquitination and proteasomal degradation of Gli2 or Gli3.<ref>PMID:14528312</ref> <ref>PMID:15897469</ref> <ref>PMID:16524876</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The E3 ligases recruit substrate proteins for targeted ubiquitylation. Recent insights into the mechanisms of ubiquitylation demonstrate that E3 ligases can possess active regulatory properties beyond those of a simple assembly scaffold. Here, we describe the dimeric structure of the E3 ligase adaptor protein SPOP (speckle-type POZ protein) in complex with the N-terminal domain of Cul3 at 2.4 A resolution. We find that SPOP forms large oligomers that can form heteromeric species with the closely related paralog SPOPL. In combination, SPOP and SPOPL (SPOP-like) form a molecular rheostat that can fine-tune E3 ubiquitin ligase activity by affecting the oligomeric state of the E3 complex. We propose that adaptor protein self-assembly provides a graded level of regulation of the SPOP/Cul3 E3 ligase toward its multiple protein substrates.
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Authors: Prive, G.G., Errington, W.J.
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Adaptor protein self-assembly drives the control of a cullin-RING ubiquitin ligase.,Errington WJ, Khan MQ, Bueler SA, Rubinstein JL, Chakrabartty A, Prive GG Structure. 2012 Jul 3;20(7):1141-53. Epub 2012 May 24. PMID:22632832<ref>PMID:22632832</ref>
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Description: Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal domain
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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 4eoz" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Cullin 3D structures|Cullin 3D structures]]
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*[[Speckle-type POZ protein 3D structures|Speckle-type POZ protein 3D structures]]
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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: Errington WJ]]
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[[Category: Prive GG]]

Current revision

Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal domain

PDB ID 4eoz

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