5tdr
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==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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