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3p8d
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3p8d is ON HOLD Authors: Cui, G., Lee, J., Thompson, J.R., Botuyan, M.V., Mer, G. Description: TUD ''Page seeded by [http://oca.weizmann.ac.il/oca...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the second Tudor domain of human PHF20 (homodimer form)== | |
| - | + | <StructureSection load='3p8d' size='340' side='right'caption='[[3p8d]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3p8d]] 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=3P8D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P8D FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3p8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p8d OCA], [https://pdbe.org/3p8d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p8d RCSB], [https://www.ebi.ac.uk/pdbsum/3p8d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p8d ProSAT]</span></td></tr> | |
| - | '' | + | </table> |
| + | == Function == | ||
| + | [https://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: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Botuyan MV]] | ||
| + | [[Category: Cui G]] | ||
| + | [[Category: Lee J]] | ||
| + | [[Category: Mer G]] | ||
| + | [[Category: Thompson JR]] | ||
Current revision
Crystal structure of the second Tudor domain of human PHF20 (homodimer form)
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Categories: Homo sapiens | Large Structures | Botuyan MV | Cui G | Lee J | Mer G | Thompson JR
