2h9m
From Proteopedia
(Difference between revisions)
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<StructureSection load='2h9m' size='340' side='right'caption='[[2h9m]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='2h9m' size='340' side='right'caption='[[2h9m]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2h9m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2h9m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Xenopus_tropicalis Xenopus tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H9M FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h9m OCA], [https://pdbe.org/2h9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h9m RCSB], [https://www.ebi.ac.uk/pdbsum/2h9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h9m ProSAT]</span></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=2h9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h9m OCA], [https://pdbe.org/2h9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h9m RCSB], [https://www.ebi.ac.uk/pdbsum/2h9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h9m ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2h9m ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2h9m ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Histone methylation at specific lysine residues brings about various downstream events that are mediated by different effector proteins. The WD40 domain of WDR5 represents a new class of histone methyl-lysine recognition domains that is important for recruiting H3K4 methyltransferases to K4-dimethylated histone H3 tail as well as for global and gene-specific K4 trimethylation. Here we report the crystal structures of full-length WDR5, WDR5Delta23 and its complexes with unmodified, mono-, di- and trimethylated histone H3K4 peptides. The structures reveal that WDR5 is able to bind all of these histone H3 peptides, but only H3K4me2 peptide forms extra interactions with WDR5 by use of both water-mediated hydrogen bonding and the altered hydrophilicity of the modified lysine 4. We propose a mechanism for the involvement of WDR5 in binding and presenting histone H3K4 for further methylation as a component of MLL complexes. | ||
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| - | Structural basis for molecular recognition and presentation of histone H3 by WDR5.,Schuetz A, Allali-Hassani A, Martin F, Loppnau P, Vedadi M, Bochkarev A, Plotnikov AN, Arrowsmith CH, Min J EMBO J. 2006 Sep 20;25(18):4245-52. Epub 2006 Aug 31. PMID:16946699<ref>PMID:16946699</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2h9m" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Allali-Hassani | + | [[Category: Xenopus tropicalis]] |
| - | [[Category: Arrowsmith | + | [[Category: Allali-Hassani A]] |
| - | [[Category: Bochkarev | + | [[Category: Arrowsmith CH]] |
| - | [[Category: Edwards | + | [[Category: Bochkarev A]] |
| - | [[Category: Loppnau | + | [[Category: Edwards AM]] |
| - | [[Category: Martin | + | [[Category: Loppnau P]] |
| - | [[Category: Min | + | [[Category: Martin F]] |
| - | [[Category: Plotnikov | + | [[Category: Min JR]] |
| - | + | [[Category: Plotnikov AN]] | |
| - | [[Category: Schuetz | + | [[Category: Schuetz A]] |
| - | [[Category: Sundstrom | + | [[Category: Sundstrom M]] |
| - | [[Category: Vedadi | + | [[Category: Vedadi M]] |
| - | [[Category: Weigelt | + | [[Category: Weigelt J]] |
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Current revision
WDR5 in complex with unmodified H3K4 peptide
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