3sd4: Difference between revisions

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-[[Image:3sd4.png|left|200px]]
+==Crystal structure of the first Tudor domain of human PHF20==
+<StructureSection load='3sd4' size='340' side='right' caption='[[3sd4]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3sd4]] is a 2 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=3SD4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SD4 FirstGlance]. <br>
+</td></tr><tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3sd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sd4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sd4 RCSB], [http://www.ebi.ac.uk/pdbsum/3sd4 PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+PHF20 is a multidomain protein and subunit of a lysine acetyltransferase complex that acetylates histone H4 and p53 but whose function is unclear. Using biochemical, biophysical and cellular approaches, we determined that PHF20 is a direct regulator of p53. A Tudor domain in PHF20 recognized p53 dimethylated at Lys370 or Lys382 and a homodimeric form of this Tudor domain could associate with the two dimethylated sites on p53 with enhanced affinity, indicating a multivalent interaction. Association with PHF20 promotes stabilization and activation of p53 by diminishing Mdm2-mediated p53 ubiquitylation and degradation. PHF20 contributes to upregulation of p53 in response to DNA damage, and ectopic expression of PHF20 in different cell lines leads to phenotypic changes that are hallmarks of p53 activation. Overall our work establishes that PHF20 functions as an effector of p53 methylation that stabilizes and activates p53.
-{{STRUCTURE_3sd4|  PDB=3sd4  |  SCENE=  }}
+PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53.,Cui G, Park S, Badeaux AI, Kim D, Lee J, Thompson JR, Yan F, Kaneko S, Yuan Z, Botuyan MV, Bedford MT, Cheng JQ, Mer G Nat Struct Mol Biol. 2012 Aug 5. doi: 10.1038/nsmb.2353. PMID:22864287<ref>PMID:22864287</ref>
-===Crystal structure of the first Tudor domain of human PHF20===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_22864287}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-[[3sd4]] is a 2 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=3SD4 OCA].
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:022864287</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
 [[Category: Botuyan, M V.]]