5tbn
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Solution NMR structure of PHF20 PHD domain in complex with a histone H3K4me2 peptide== | |
- | + | <StructureSection load='5tbn' size='340' side='right' caption='[[5tbn]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[5tbn]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TBN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TBN FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
- | [[Category: | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=5tbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tbn OCA], [http://pdbe.org/5tbn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tbn RCSB], [http://www.ebi.ac.uk/pdbsum/5tbn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tbn ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/PHF20_HUMAN PHF20_HUMAN]] Methyllysine-binding protein, component of the MOF histone acetyltransferase protein complex. Not required for maintaining the global histone H4 'Lys-16' acetylation (H4K16ac) levels or locus specific histone acetylation, but instead works downstream in transcriptional regulation of MOF target genes (By similarity). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. Contributes to methyllysine-dependent p53/TP53 stabilization and up-regulation after DNA damage.<ref>PMID:20018852</ref> <ref>PMID:22864287</ref> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Botuyan, M V]] | ||
[[Category: Cui, G]] | [[Category: Cui, G]] | ||
[[Category: Mer, G]] | [[Category: Mer, G]] | ||
- | [[Category: | + | [[Category: Methylated lysine]] |
+ | [[Category: Phd finger]] | ||
+ | [[Category: Transcription - structural protein complex]] |
Revision as of 17:46, 19 October 2016
Solution NMR structure of PHF20 PHD domain in complex with a histone H3K4me2 peptide
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