5znp: Difference between revisions

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'''Unreleased structure'''


The entry 5znp is ON HOLD  until Paper Publication
==Crystal structure of PtSHL in complex with an H3K4me3 peptide==
<StructureSection load='5znp' size='340' side='right' caption='[[5znp]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5znp]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZNP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZNP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=M3L:N-TRIMETHYLLYSINE'>M3L</scene></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=5znp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5znp OCA], [http://pdbe.org/5znp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5znp RCSB], [http://www.ebi.ac.uk/pdbsum/5znp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5znp ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The ability of a cell to dynamically switch its chromatin between different functional states constitutes a key mechanism regulating gene expression. Histone mark "readers" display distinct binding specificity to different histone modifications and play critical roles in regulating chromatin states. Here, we show a plant-specific histone reader SHORT LIFE (SHL) capable of recognizing both H3K27me3 and H3K4me3 via its bromo-adjacent homology (BAH) and plant homeodomain (PHD) domains, respectively. Detailed biochemical and structural studies suggest a binding mechanism that is mutually exclusive for either H3K4me3 or H3K27me3. Furthermore, we show a genome-wide co-localization of SHL with H3K27me3 and H3K4me3, and that BAH-H3K27me3 and PHD-H3K4me3 interactions are important for SHL-mediated floral repression. Together, our study establishes BAH-PHD cassette as a dual histone methyl-lysine binding module that is distinct from others in recognizing both active and repressive histone marks.


Authors:  
Dual recognition of H3K4me3 and H3K27me3 by a plant histone reader SHL.,Qian S, Lv X, Scheid RN, Lu L, Yang Z, Chen W, Liu R, Boersma MD, Denu JM, Zhong X, Du J Nat Commun. 2018 Jun 21;9(1):2425. doi: 10.1038/s41467-018-04836-y. PMID:29930355<ref>PMID:29930355</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5znp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Du, J]]
[[Category: Lv, X]]
[[Category: Bah]]
[[Category: Epigenetic]]
[[Category: Gene regulation]]
[[Category: H3k4me3]]
[[Category: Phd]]
[[Category: Plant]]
[[Category: Shl]]
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