3sd4: Difference between revisions

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==Crystal structure of the first Tudor domain of human PHF20==
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<StructureSection load='3sd4' size='340' side='right'caption='[[3sd4]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3sd4]] 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=3SD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SD4 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.928&#8491;</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=3sd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sd4 OCA], [https://pdbe.org/3sd4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sd4 RCSB], [https://www.ebi.ac.uk/pdbsum/3sd4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sd4 ProSAT]</span></td></tr>
{{STRUCTURE_3sd4|  PDB=3sd4  |  SCENE=  }}
</table>
 
== Function ==
===Crystal structure of the first Tudor domain of human PHF20===
[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>
 
== 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>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Botuyan, M V.]]
[[Category: Large Structures]]
[[Category: Cui, G.]]
[[Category: Botuyan MV]]
[[Category: Mer, G.]]
[[Category: Cui G]]
[[Category: Thompson, J R.]]
[[Category: Mer G]]
[[Category: Transcription]]
[[Category: Thompson JR]]
[[Category: Tudor domain]]

Latest revision as of 12:49, 1 March 2024

Crystal structure of the first Tudor domain of human PHF20Crystal structure of the first Tudor domain of human PHF20

Structural highlights

3sd4 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 1.928Å
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]

References

  1. ↑ 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
  2. ↑ 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

3sd4, resolution 1.93Å

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