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2H68

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

Summary for 2H68
Entry DOI10.2210/pdb2h68/pdb
Related2CNX 2CO0 2H6K 2H6N 2H6Q
DescriptorWD-repeat protein 5 (2 entities in total)
Functional Keywordswd40 wd-repeat histone modification chromatin, gene regulation
Biological sourceHomo sapiens (human)
Cellular locationNucleus: P61964
Total number of polymer chains2
Total formula weight68607.83
Authors
Ruthenburg, A.J.,Wang, W.-K.,Graybosch, D.M.,Li, H.,Allis, C.D.,Patel, D.J.,Verdine, G.L. (deposition date: 2006-05-30, release date: 2006-07-04, Last modification date: 2023-08-30)
Primary citationRuthenburg, A.J.,Wang, W.-K.,Graybosch, D.M.,Li, H.,Allis, C.D.,Patel, D.J.,Verdine, G.L.
Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex.
Nat.Struct.Mol.Biol., 13:704-712, 2006
Cited by
PubMed Abstract: 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.
PubMed: 16829959
DOI: 10.1038/nsmb1119
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.79 Å)
Structure validation

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