4ql1

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<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=4ql1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ql1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ql1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ql1 PDBsum]</span></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=4ql1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ql1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ql1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ql1 PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[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>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 05:39, 25 December 2014

Crystal structure of human WDR5 in complex with compound OICR-9429

4ql1, resolution 1.50Å

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