5hqg

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==WD40 domain of Human E3 Ubiquitin Ligase COP1 (RFWD2)==
==WD40 domain of Human E3 Ubiquitin Ligase COP1 (RFWD2)==
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<StructureSection load='5hqg' size='340' side='right' caption='[[5hqg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='5hqg' size='340' side='right'caption='[[5hqg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5hqg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HQG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HQG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5hqg]] 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=5HQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HQG FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5hqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hqg OCA], [http://pdbe.org/5hqg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hqg RCSB], [http://www.ebi.ac.uk/pdbsum/5hqg PDBsum]</span></td></tr>
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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&#8491;</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=5hqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hqg OCA], [https://pdbe.org/5hqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hqg RCSB], [https://www.ebi.ac.uk/pdbsum/5hqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hqg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/RFWD2_HUMAN RFWD2_HUMAN]] E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1. Involved in 14-3-3 protein sigma/SFN ubiquitination and proteasomal degradation, leading to AKT activation and promotion of cell survival. Ubiquitinates MTA1 leading to its proteasomal degradation.<ref>PMID:12466024</ref> <ref>PMID:12615916</ref> <ref>PMID:14739464</ref> <ref>PMID:15103385</ref> <ref>PMID:19805145</ref> <ref>PMID:19837670</ref> <ref>PMID:21625211</ref>
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[https://www.uniprot.org/uniprot/COP1_HUMAN COP1_HUMAN] E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1. Involved in 14-3-3 protein sigma/SFN ubiquitination and proteasomal degradation, leading to AKT activation and promotion of cell survival. Ubiquitinates MTA1 leading to its proteasomal degradation. Upon binding to TRIB1, ubiquitinates CEBPA, which lacks a canonical COP1-binding motif (Probable).<ref>PMID:12466024</ref> <ref>PMID:12615916</ref> <ref>PMID:14739464</ref> <ref>PMID:15103385</ref> <ref>PMID:19805145</ref> <ref>PMID:19837670</ref> <ref>PMID:21625211</ref> <ref>PMID:27041596</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5hqg" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5hqg" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Blacklow, S C]]
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[[Category: Homo sapiens]]
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[[Category: Uljon, S]]
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[[Category: Large Structures]]
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[[Category: Hydrolase]]
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[[Category: Blacklow SC]]
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[[Category: Wd40 domain e3 ligase]]
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[[Category: Uljon S]]

Current revision

WD40 domain of Human E3 Ubiquitin Ligase COP1 (RFWD2)

PDB ID 5hqg

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