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4qqe

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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=4qqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qqe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qqe RCSB], [http://www.ebi.ac.uk/pdbsum/4qqe 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=4qqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qqe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qqe RCSB], [http://www.ebi.ac.uk/pdbsum/4qqe 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/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Al-Awar, R.]]
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[[Category: Al-Awar, R]]
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[[Category: Arrowsmith, C H.]]
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[[Category: Arrowsmith, C H]]
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[[Category: Bountra, C.]]
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[[Category: Bountra, C]]
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[[Category: Brown, P J.]]
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[[Category: Brown, P J]]
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[[Category: Dombrovski, L.]]
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[[Category: Dombrovski, L]]
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[[Category: Dong, A.]]
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[[Category: Dong, A]]
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[[Category: Edwards, A M.]]
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[[Category: Edwards, A M]]
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[[Category: Getlik, M.]]
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[[Category: Getlik, M]]
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[[Category: Poda, G.]]
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[[Category: Poda, G]]
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[[Category: SGC, Structural Genomics Consortium.]]
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[[Category: Schapira, M.]]
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[[Category: Senisterra, G.]]
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[[Category: Smil, D.]]
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[[Category: Vedadi, M.]]
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[[Category: Wernimont, A.]]
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[[Category: Wu, H.]]
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[[Category: Sgc]]
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
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[[Category: Structural genomics consortium]]
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[[Category: Schapira, M]]
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[[Category: Senisterra, G]]
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[[Category: Smil, D]]
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[[Category: Vedadi, M]]
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[[Category: Wernimont, A]]
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[[Category: Wu, H]]
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[[Category: Sgc]]
[[Category: Transcription]]
[[Category: Transcription]]
[[Category: Wdr5]]
[[Category: Wdr5]]

Revision as of 12:52, 25 December 2014

Crystal structure of WDR5, WD repeat domain 5 in complex with compound SGC-DS-MT-0345

4qqe, resolution 1.80Å

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