3p8d

From Proteopedia

(Difference between revisions)

Current revision

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

Structural highlights

3p8d is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2]

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Cai Y, Jin J, Swanson SK, Cole MD, Choi SH, Florens L, Washburn MP, Conaway JW, Conaway RC. Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex. J Biol Chem. 2010 Feb 12;285(7):4268-72. doi: 10.1074/jbc.C109.087981. Epub 2009 , Dec 14. PMID:20018852 doi:10.1074/jbc.C109.087981
↑ 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. PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53. Nat Struct Mol Biol. 2012 Aug 5. doi: 10.1038/nsmb.2353. PMID:22864287 doi:10.1038/nsmb.2353
↑ 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. PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53. Nat Struct Mol Biol. 2012 Aug 5. doi: 10.1038/nsmb.2353. PMID:22864287 doi:10.1038/nsmb.2353

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Crystal structure of the second Tudor domain of human PHF20 (homodimer form)==
-<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 ==
-<table><tr><td colspan='2'>[[3p8d]] 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=3P8D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3p8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p8d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3p8d RCSB], [http://www.ebi.ac.uk/pdbsum/3p8d PDBsum]</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>
+== 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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 13: / Line 17: @@
 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/>
@@ Line 18: / Line 23: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Botuyan, M V]]
+[[Category: Large Structures]]
-[[Category: Cui, G]]
+[[Category: Botuyan MV]]
-[[Category: Lee, J]]
+[[Category: Cui G]]
-[[Category: Mer, G]]
+[[Category: Lee J]]
-[[Category: Thompson, J R]]
+[[Category: Mer G]]
-[[Category: Histone binding]]
+[[Category: Thompson JR]]
-[[Category: Lysine-methylated p53 binding]]
-[[Category: Protein binding]]
-[[Category: Tudor domain]]

3p8d

From Proteopedia

Current revision

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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