3p8d

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='3p8d' size='340' side='right'caption='[[3p8d]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3p8d' size='340' side='right'caption='[[3p8d]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3p8d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>
+
<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='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>
+
</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&#8491;</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>
</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>
-
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.
+
-
 
+
-
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>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3p8d" style="background-color:#fffaf0;"></div>
+
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Human]]
+
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Botuyan, M V]]
+
[[Category: Botuyan MV]]
-
[[Category: Cui, G]]
+
[[Category: Cui G]]
-
[[Category: Lee, J]]
+
[[Category: Lee J]]
-
[[Category: Mer, G]]
+
[[Category: Mer G]]
-
[[Category: Thompson, J R]]
+
[[Category: Thompson JR]]
-
[[Category: Histone binding]]
+
-
[[Category: Lysine-methylated p53 binding]]
+
-
[[Category: Protein binding]]
+
-
[[Category: Tudor domain]]
+

Revision as of 11:21, 21 February 2024

Crystal structure of the second Tudor domain of human PHF20 (homodimer form)

PDB ID 3p8d

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3p8d"
Personal tools