View source for 1e0n


==YJQ8WW domain from Saccharomyces cerevisae==
<StructureSection load='1e0n' size='340' side='right'caption='[[1e0n]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1e0n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E0N FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1e0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0n OCA], [https://pdbe.org/1e0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e0n RCSB], [https://www.ebi.ac.uk/pdbsum/1e0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e0n ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SET2_YEAST SET2_YEAST] Histone methyltransferase that trimethylates histone H3 'Lys-36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression. The methyltransferase activity requires the recruitment to the RNA polymerase II, which is CTK1 dependent.<ref>PMID:11839797</ref> <ref>PMID:12629047</ref> <ref>PMID:12736296</ref> <ref>PMID:12773564</ref> <ref>PMID:12917322</ref> <ref>PMID:15798214</ref> <ref>PMID:16227595</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Two new NMR structures of WW domains, the mouse formin binding protein and a putative 84.5 kDa protein from Saccharomyces cerevisiae, show that this domain, only 35 amino acids in length, defines the smallest monomeric triple-stranded antiparallel beta-sheet protein domain that is stable in the absence of disulfide bonds, tightly bound ions or ligands. The structural roles of conserved residues have been studied using site-directed mutagenesis of both wild type domains. Crucial interactions responsible for the stability of the WW structure have been identified. Based on a network of highly conserved long range interactions across the beta-sheet structure that supports the WW fold and on a systematic analysis of conserved residues in the WW family, we have designed a folded prototype WW sequence.

Structural analysis of WW domains and design of a WW prototype.,Macias MJ, Gervais V, Civera C, Oschkinat H Nat Struct Biol. 2000 May;7(5):375-9. PMID:10802733<ref>PMID:10802733</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1e0n" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Civera C]]
[[Category: Gervais V]]
[[Category: Macias MJ]]
[[Category: Oschkinat H]]