3q1j

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Crystal structure of tudor domain 1 of human PHD finger protein 20

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 ==Crystal structure of tudor domain 1 of human PHD finger protein 20==
-<StructureSection load='3q1j' size='340' side='right' caption='[[3q1j]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
+<StructureSection load='3q1j' size='340' side='right'caption='[[3q1j]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3q1j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q1J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q1J FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3q1j]] is a 1 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=3Q1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q1J FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
-<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 Homo sapiens])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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=3q1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q1j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q1j RCSB], [http://www.ebi.ac.uk/pdbsum/3q1j PDBsum]</span></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=3q1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q1j OCA], [https://pdbe.org/3q1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q1j RCSB], [https://www.ebi.ac.uk/pdbsum/3q1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q1j ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[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>
-The human PHD finger protein 20 (PHF20) is a putative transcription factor. While little is known about its cognate cellular role, antibodies against PHF20 are present in sera from patients with hepatocellular carcinoma, glioblastoma and childhood medulloblastula. PHF20 comprises two N-terminal Tudor domains, a central C2H2-link zinc finger domain and a C-terminal zinc-binding PHD domain, and is a component of some MLL methyltransferase complexes. Here, we report the crystal structures of the N-terminal Tudor domains of PHF20 and highlight the novel structural features of each domain. We also confirm previous studies suggesting that the second Tudor domain of PHF20 exhibits preference for dimethylated histone substrates.
-Crystal structures of the Tudor domains of human PHF20 reveal novel structural variations on the Royal Family of proteins.,Adams-Cioaba MA, Li Z, Tempel W, Guo Y, Bian C, Li Y, Lam R, Min J FEBS Lett. 2012 Mar 23;586(6):859-65. Epub 2012 Feb 24. PMID:22449972<ref>PMID:22449972</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 == References ==
 <references/>
@@ Line 20: / Line 15: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Arrowsmith, C H]]
+[[Category: Large Structures]]
-[[Category: Bian, C]]
+[[Category: Arrowsmith CH]]
-[[Category: Bountra, C]]
+[[Category: Bian C]]
-[[Category: Chao, X]]
+[[Category: Bountra C]]
-[[Category: Crombet, L]]
+[[Category: Chao X]]
-[[Category: Edwards, A M]]
+[[Category: Crombet L]]
-[[Category: Lam, R]]
+[[Category: Edwards AM]]
-[[Category: Li, Z]]
+[[Category: Lam R]]
-[[Category: Min, J]]
+[[Category: Li Z]]
-[[Category: Structural genomic]]
+[[Category: Min J]]
-[[Category: Tempel, W]]
+[[Category: Tempel W]]
-[[Category: Weigelt, J]]
+[[Category: Weigelt J]]
-[[Category: Wernimont, A K]]
+[[Category: Wernimont AK]]
-[[Category: Mbt]]
-[[Category: Sgc]]
-[[Category: Transcription]]
-[[Category: Tudor domain]]

3q1j

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Crystal structure of tudor domain 1 of human PHD finger protein 20

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Function

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