3emh

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[[Image:3emh.png|left|200px]]
 
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{{STRUCTURE_3emh| PDB=3emh | SCENE= }}
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==Structural basis of WDR5-MLL interaction==
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<StructureSection load='3emh' size='340' side='right'caption='[[3emh]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3emh]] 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=3EMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EMH 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]] 1.37&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3emh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3emh OCA], [https://pdbe.org/3emh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3emh RCSB], [https://www.ebi.ac.uk/pdbsum/3emh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3emh ProSAT]</span></td></tr>
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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/em/3emh_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=3emh 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 component of the mixed lineage leukemia (MLL) complex, which methylates lysine 4 of histone H3, and was identified as a methylated Lys-4 histone H3-binding protein. Here, we present a crystal structure of WDR5 bound to an MLL peptide. Surprisingly, we find that WDR5 utilizes the same pocket shown to bind histone H3 for this MLL interaction. Furthermore, the WDR5-MLL interaction is disrupted preferentially by mono- and di-methylated Lys-4 histone H3 over unmodified and tri-methylated Lys-4 histone H3. These data implicate a delicate interplay between the effector, WDR5, the catalytic subunit, MLL, and the substrate, histone H3, of the MLL complex. We suggest that the activity of the MLL complex might be regulated through this interplay.
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===Structural basis of WDR5-MLL interaction===
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WDR5 interacts with mixed lineage leukemia (MLL) protein via the histone H3-binding pocket.,Song JJ, Kingston RE J Biol Chem. 2008 Dec 12;283(50):35258-64. Epub 2008 Oct 7. PMID:18840606<ref>PMID:18840606</ref>
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{{ABSTRACT_PUBMED_18840606}}
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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 3emh" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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[[3emh]] is a 2 chain structure with sequence 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=3EMH OCA].
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*[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:018840606</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Kingston, R E.]]
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[[Category: Large Structures]]
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[[Category: Song, J J.]]
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[[Category: Kingston RE]]
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[[Category: Chromatin]]
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[[Category: Song JJ]]
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[[Category: Gene regulation]]
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[[Category: Histone]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Wd repeat]]
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[[Category: Wd40 repeat]]
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[[Category: Zinc-finger]]
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Current revision

Structural basis of WDR5-MLL interaction

PDB ID 3emh

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