View source for 5tdw


==Set3 PHD finger in complex with histone H3K4me3==
<StructureSection load='5tdw' size='340' side='right'caption='[[5tdw]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5tdw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TDW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5tdw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tdw OCA], [https://pdbe.org/5tdw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tdw RCSB], [https://www.ebi.ac.uk/pdbsum/5tdw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tdw ProSAT]</span></td></tr>
</table>
== Function ==
[https://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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5tdw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Ali M]]
[[Category: Andrews FH]]
[[Category: Kutateladze TG]]