6oi0: Difference between revisions

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-'''Unreleased structure'''
-The entry 6oi0 is ON HOLD  until Paper Publication
+==Crystal structure of human WDR5 in complex with L-arginine==
+<StructureSection load='6oi0' size='340' side='right'caption='[[6oi0]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6oi0]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OI0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OI0 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6oi0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oi0 OCA], [http://pdbe.org/6oi0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oi0 RCSB], [http://www.ebi.ac.uk/pdbsum/6oi0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oi0 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/WDR5_HUMAN WDR5_HUMAN]] Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4'. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation.<ref>PMID:19556245</ref> <ref>PMID:19103755</ref> <ref>PMID:20018852</ref> <ref>PMID:16600877</ref> <ref>PMID:16829960</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Histone H3 arginine 2 (H3R2) is post-translationally modified in three different states by "writers" of the protein arginine methyltransferase (PRMT) family. H3R2 methylarginine isoforms include PRMT5-catalyzed monomethylation (me1) and symmetric dimethylation (me2s), and PRMT6-catalyzed me1 and asymmetric dimethylation (me2a). WD-40 repeat-containing protein 5 (WDR5) is an epigenetic "reader" protein that interacts with H3R2. Previous studies suggested that H3R2me2s specified a high-affinity interaction with WDR5. However, our prior biological data prompted the hypothesis that WDR5 may also interact with H3R2me1. Here, using highly accurate quantitative binding analysis combined with high-resolution crystal structures of WDR5 in complex with unmodified (me0) and me1/me2s L-Arginine amino acids and in complex with H3R2me1 peptide, we provide a rigorous biochemical study and address long-standing discrepancies of this important biological interaction. Despite modest structural differences at the binding interface, our study supports an interaction model regulated by a binary arginine methylation switch: H3R2me2a prevents interaction with WDR5, whereas H3R2me0/me1/me2s are equally permissive.
-Authors: Lorton, B.M., Harijan, R.K., Burgos, E., Bonanno, J.B., Almo, S.C., Shechter, D.
+A binary arginine methylation switch on histone H3 Arginine 2 regulates its interaction with WDR5.,Lorton BM, Harijan RK, Burgos ES, Bonanno JB, Almo SC, Shechter D Biochemistry. 2020 Mar 24. doi: 10.1021/acs.biochem.0c00035. PMID:32207970<ref>PMID:32207970</ref>
-Description: Crystal structure of human WDR5 in complex with L-arginine
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Almo, S.C]]
+<div class="pdbe-citations 6oi0" style="background-color:#fffaf0;"></div>
-[[Category: Harijan, R.K]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Almo, S C]]
+[[Category: Bonanno, J B]]
+[[Category: Burgos, E]]
+[[Category: Harijan, R K]]
+[[Category: Lorton, B M]]
 [[Category: Shechter, D]]
-[[Category: Lorton, B.M]]
+[[Category: Chromatin]]
-[[Category: Burgos, E]]
+[[Category: Epigenetic]]
-[[Category: Bonanno, J.B]]
+[[Category: Gene regulation]]
+[[Category: Methylarginine]]
+[[Category: Methylation]]
+[[Category: Post-translational modification]]