9jkb

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m (Protected "9jkb" [edit=sysop:move=sysop])
Current revision (07:14, 23 October 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9jkb is ON HOLD
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==Cryo-EM structure of the CUL1-RBX1-SKP1-FBXO4 SCF ubiquition ligase complex==
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<StructureSection load='9jkb' size='340' side='right'caption='[[9jkb]], [[Resolution|resolution]] 3.93&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9jkb]] is a 5 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=9JKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9JKB FirstGlance]. <br>
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Description:
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.93&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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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=9jkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9jkb OCA], [https://pdbe.org/9jkb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9jkb RCSB], [https://www.ebi.ac.uk/pdbsum/9jkb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9jkb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RBX1_HUMAN RBX1_HUMAN] E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme, like CDC34, to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M.<ref>PMID:10579999</ref> <ref>PMID:11027288</ref> <ref>PMID:16751180</ref> <ref>PMID:16678110</ref> <ref>PMID:19679664</ref>
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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: Xu C]]
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[[Category: Zhu W]]

Current revision

Cryo-EM structure of the CUL1-RBX1-SKP1-FBXO4 SCF ubiquition ligase complex

PDB ID 9jkb

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