3sd4
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3sd4 is ON HOLD Authors: Cui, G., Botuyan, M.V., Thompson, J.R., Mer, G. Description: Not Available) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the first Tudor domain of human PHF20== | |
| - | + | <StructureSection load='3sd4' size='340' side='right'caption='[[3sd4]], [[Resolution|resolution]] 1.93Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3sd4]] 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=3SD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SD4 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]] 1.928Å</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=3sd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sd4 OCA], [https://pdbe.org/3sd4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sd4 RCSB], [https://www.ebi.ac.uk/pdbsum/3sd4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sd4 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: Mer G]] | ||
| + | [[Category: Thompson JR]] | ||
Current revision
Crystal structure of the first Tudor domain of human PHF20
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