5tdr: Difference between revisions
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==Set3 PHD finger in complex with histone H3K4me2== | |||
<StructureSection load='5tdr' size='340' side='right' caption='[[5tdr]], [[Resolution|resolution]] 1.42Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5tdr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TDR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TDR FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tdw|5tdw]]</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=5tdr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tdr OCA], [http://pdbe.org/5tdr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tdr RCSB], [http://www.ebi.ac.uk/pdbsum/5tdr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tdr ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/SET3_YEAST SET3_YEAST]] Transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. Required for both gene activation and repression. Part of the Set3C complex, which is required to repress early/middle sporulation genes during meiosis. Required for the transcriptional activation of genes with high activity.<ref>PMID:12434058</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The plant homeodomain (PHD) finger of Set3 binds methylated lysine 4 of histone H3 in vitro and in vivo; however, precise selectivity of this domain has not been fully characterized. Here, we explore the determinants of methyllysine recognition by the PHD fingers of Set3 and its orthologs. We use X-ray crystallographic and spectroscopic approaches to show that the Set3 PHD finger binds di- and trimethylated states of H3K4 with comparable affinities and employs similar molecular mechanisms to form complexes with either mark. Composition of the methyllysine-binding pocket plays an essential role in determining the selectivity of the PHD fingers. The finding that the histone-binding activity is not conserved in the PHD finger of Set4 suggests different functions for the Set3 and Set4 paralogs. | |||
Structural Insight into Recognition of Methylated Histone H3K4 by Set3.,Gatchalian J, Ali M, Andrews FH, Zhang Y, Barrett AS, Kutateladze TG J Mol Biol. 2016 Sep 30. pii: S0022-2836(16)30400-4. doi:, 10.1016/j.jmb.2016.09.020. PMID:27697561<ref>PMID:27697561</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5tdr" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ali, M]] | [[Category: Ali, M]] | ||
[[Category: Andrews, F | [[Category: Andrews, F H]] | ||
[[Category: Kutateladze, T G]] | |||
[[Category: Epigenetic]] | |||
[[Category: Histone]] | |||
[[Category: Methylation]] | |||
[[Category: Transcription]] | |||
Revision as of 18:21, 2 November 2016
Set3 PHD finger in complex with histone H3K4me2
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