4ppe

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(New page: '''Unreleased structure''' The entry 4ppe is ON HOLD Authors: Perry, J.J., Arvai, A.S., Hitomi, C., Tainer, J.A. Description: human RNF4 RING domain)
Current revision (12:42, 1 March 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 4ppe is ON HOLD
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==human RNF4 RING domain==
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<StructureSection load='4ppe' size='340' side='right'caption='[[4ppe]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4ppe]] is a 2 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=4PPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PPE FirstGlance]. <br>
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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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4ppe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ppe OCA], [https://pdbe.org/4ppe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ppe RCSB], [https://www.ebi.ac.uk/pdbsum/4ppe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ppe ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RNF4_HUMAN RNF4_HUMAN] E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation.<ref>PMID:12885770</ref> <ref>PMID:18408734</ref> <ref>PMID:19307308</ref> <ref>PMID:20212317</ref> <ref>PMID:20943951</ref> <ref>PMID:20026589</ref>
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Authors: Perry, J.J., Arvai, A.S., Hitomi, C., Tainer, J.A.
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==See Also==
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*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
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Description: human RNF4 RING domain
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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: Arvai AS]]
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[[Category: Hitomi C]]
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[[Category: Perry JJ]]
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[[Category: Tainer JA]]

Current revision

human RNF4 RING domain

PDB ID 4ppe

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