2h68

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{{Seed}}
 
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[[Image:2h68.png|left|200px]]
 
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==Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex==
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The line below this paragraph, containing "STRUCTURE_2h68", creates the "Structure Box" on the page.
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<StructureSection load='2h68' size='340' side='right'caption='[[2h68]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2h68]] is a 2 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=2H68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H68 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.79&#8491;</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=2h68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h68 OCA], [https://pdbe.org/2h68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h68 RCSB], [https://www.ebi.ac.uk/pdbsum/2h68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h68 ProSAT]</span></td></tr>
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{{STRUCTURE_2h68| PDB=2h68 | SCENE= }}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h6/2h68_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2h68 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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WDR5 is a core component of SET1-family complexes that achieve transcriptional activation via methylation of histone H3 on Nzeta of Lys4 (H3K4). The role of WDR5 in the MLL1 complex has recently been described as specific recognition of dimethyl-K4 in the context of a histone H3 amino terminus; WDR5 is essential for vertebrate development, Hox gene activation and global H3K4 trimethylation. We report the high-resolution X-ray structures of WDR5 in the unliganded form and complexed with histone H3 peptides having unmodified and mono-, di- and trimethylated K4, which together provide the first comprehensive analysis of methylated histone recognition by the ubiquitous WD40-repeat fold. Contrary to predictions, the structures reveal that WDR5 does not read out the methylation state of K4 directly, but instead serves to present the K4 side chain for further methylation by SET1-family complexes.
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===Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex===
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Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex.,Ruthenburg AJ, Wang W, Graybosch DM, Li H, Allis CD, Patel DJ, Verdine GL Nat Struct Mol Biol. 2006 Aug;13(8):704-12. Epub 2006 Jul 9. PMID:16829959<ref>PMID:16829959</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2h68" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_16829959}}, adds the Publication Abstract to the page
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*[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 16829959 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16829959}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2H68 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H68 OCA].
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==Reference==
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<ref group="xtra">PMID:16829959</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Allis, C D.]]
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[[Category: Large Structures]]
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[[Category: Graybosch, D M.]]
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[[Category: Allis CD]]
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[[Category: Li, H.]]
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[[Category: Graybosch DM]]
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[[Category: Patel, D J.]]
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[[Category: Li H]]
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[[Category: Ruthenburg, A J.]]
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[[Category: Patel DJ]]
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[[Category: Verdine, G L.]]
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[[Category: Ruthenburg AJ]]
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[[Category: Wang, W K.]]
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[[Category: Verdine GL]]
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[[Category: Wd40 wd-repeat histone modification chromatin]]
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[[Category: Wang W-K]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 09:52:26 2009''
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Current revision

Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex

PDB ID 2h68

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