5in1
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of the MRG701 chromodomain== | |
| + | <StructureSection load='5in1' size='340' side='right'caption='[[5in1]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5in1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IN1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IN1 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]] 1.4Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5in1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5in1 OCA], [https://pdbe.org/5in1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5in1 RCSB], [https://www.ebi.ac.uk/pdbsum/5in1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5in1 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q2R2X7_ORYSJ Q2R2X7_ORYSJ] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | MRG proteins are conserved during evolution in fungi, flies, mammals and plants, and they can exhibit diversified functions. The animal MRGs were found to form various complexes to activate gene expression. Plant MRG1/2 and MRG702 were reported to be involved in the regulation of flowering time via binding to H3K36me3-marked flowering genes. Herein, we determined the crystal structure of MRG701 chromodomain (MRG701CD). MRG701CD forms a novel dimerization fold both in crystal and in solution. Moreover, we found that the dimerization of MRG chromodomains is conserved in green plants. Our findings may provide new insights into the mechanism of MRGs in regulation of gene expression in green plants. | ||
| - | + | Structural studies on MRG701 chromodomain reveal a novel dimerization interface of MRG proteins in green plants.,Liu Y, Wu H, Yu Y, Huang Y Protein Cell. 2016 Nov;7(11):792-803. Epub 2016 Sep 8. PMID:27638467<ref>PMID:27638467</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5in1" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Oryza sativa]] | ||
| + | [[Category: Huang Y]] | ||
| + | [[Category: Liu Y]] | ||
Current revision
Crystal Structure of the MRG701 chromodomain
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