6ofz
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6ofz is ON HOLD Authors: Lorton, B.M., Harijan, R.K., Burgos, E., Bonanno, J.B., Almo, S.C., Shechter, D. Description: Crystal structure of human W...) |
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of human WDR5== | |
+ | <StructureSection load='6ofz' size='340' side='right'caption='[[6ofz]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6ofz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OFZ 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]] 1.85Å</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=6ofz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ofz OCA], [https://pdbe.org/6ofz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ofz RCSB], [https://www.ebi.ac.uk/pdbsum/6ofz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ofz ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://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. | ||
- | + | 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> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 6ofz" style="background-color:#fffaf0;"></div> |
- | [[Category: Almo | + | |
- | [[Category: Burgos | + | ==See Also== |
- | [[Category: | + | *[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]] |
- | [[Category: | + | == References == |
- | [[Category: Shechter | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Almo SC]] | ||
+ | [[Category: Bonanno JB]] | ||
+ | [[Category: Burgos E]] | ||
+ | [[Category: Harijan RK]] | ||
+ | [[Category: Lorton BM]] | ||
+ | [[Category: Shechter D]] |
Current revision
Crystal structure of human WDR5
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Categories: Homo sapiens | Large Structures | Almo SC | Bonanno JB | Burgos E | Harijan RK | Lorton BM | Shechter D