5tbn

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==Solution NMR structure of PHF20 PHD domain in complex with a histone H3K4me2 peptide==
==Solution NMR structure of PHF20 PHD domain in complex with a histone H3K4me2 peptide==
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<StructureSection load='5tbn' size='340' side='right'caption='[[5tbn]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='5tbn' size='340' side='right'caption='[[5tbn]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5tbn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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>
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<table><tr><td colspan='2'>[[5tbn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5TBN FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
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<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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PHF20, C20orf104, GLEA2, HCA58, NZF, TZP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5tbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tbn OCA], [https://pdbe.org/5tbn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tbn RCSB], [https://www.ebi.ac.uk/pdbsum/5tbn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tbn ProSAT]</span></td></tr>
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<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>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Botuyan, M V]]
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[[Category: Botuyan MV]]
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[[Category: Cui, G]]
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[[Category: Cui G]]
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[[Category: Mer, G]]
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[[Category: Mer G]]
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[[Category: Methylated lysine]]
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[[Category: Phd finger]]
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[[Category: Transcription - structural protein complex]]
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Current revision

Solution NMR structure of PHF20 PHD domain in complex with a histone H3K4me2 peptide

PDB ID 5tbn

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