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==Crystal structure of WDR5 in complex with MYC MbIIIb peptide==
==Crystal structure of WDR5 in complex with MYC MbIIIb peptide==
<StructureSection load='4y7r' size='340' side='right' caption='[[4y7r]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='4y7r' size='340' side='right'caption='[[4y7r]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4y7r]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y7R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y7R FirstGlance]. <br>
<table><tr><td colspan='2'>[[4y7r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y7R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y7R FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.898&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">WDR5, BIG3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=4y7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y7r OCA], [http://pdbe.org/4y7r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y7r RCSB], [http://www.ebi.ac.uk/pdbsum/4y7r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y7r 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=4y7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y7r OCA], [https://pdbe.org/4y7r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y7r RCSB], [https://www.ebi.ac.uk/pdbsum/4y7r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y7r ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
[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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4y7r" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4y7r" style="background-color:#fffaf0;"></div>
==See Also==
*[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Fesik, S W]]
[[Category: Large Structures]]
[[Category: Olejniczak, E T]]
[[Category: Synthetic construct]]
[[Category: Phan, J]]
[[Category: Fesik SW]]
[[Category: Sun, Q]]
[[Category: Olejniczak ET]]
[[Category: Tansey, W P]]
[[Category: Phan J]]
[[Category: Thomas, L R]]
[[Category: Sun Q]]
[[Category: Dna binding protein]]
[[Category: Tansey WP]]
[[Category: Myc wdr5 cancer]]
[[Category: Thomas LR]]
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