5znr
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of PtSHL in complex with an H3K27me3 peptide== | |
| + | <StructureSection load='5znr' size='340' side='right' caption='[[5znr]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5znr]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZNR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZNR FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=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=5znr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5znr OCA], [http://pdbe.org/5znr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5znr RCSB], [http://www.ebi.ac.uk/pdbsum/5znr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5znr 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5znr" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Du, J]] | ||
| + | [[Category: Lv, X]] | ||
| + | [[Category: Bah]] | ||
| + | [[Category: Epigenetic]] | ||
| + | [[Category: Gene regulation]] | ||
| + | [[Category: H3k27me3]] | ||
| + | [[Category: Phd]] | ||
| + | [[Category: Plant]] | ||
| + | [[Category: Shl]] | ||
Revision as of 07:32, 18 July 2018
Crystal structure of PtSHL in complex with an H3K27me3 peptide
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Categories: Du, J | Lv, X | Bah | Epigenetic | Gene regulation | H3k27me3 | Phd | Plant | Shl
