2H6Q

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

Summary for 2H6Q

• Entry DOI: 10.2210/pdb2h6q/pdb
• Related: 2CNX 2CO0 2H68 2H6K 2H6N
• Descriptor: WD-repeat protein 5, Histone H3 K4-Me3 9-residue peptide (3 entities in total)
• Functional Keywords: wdr5 wd40 wd-repeat histone h3 modification mll set chromatin, gene regulation
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P61964
• Total number of polymer chains: 4
• Total formula weight: 70818.50

Authors

Ruthenburg, A.J.,Wang, W.-K.,Graybosch, D.M.,Li, H.,Allis, C.D.,Patel, D.J.,Verdine, G.L. (deposition date: 2006-06-01, release date: 2006-07-04, Last modification date: 2023-08-30)

Primary citation

Ruthenburg, 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

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

Experimental method

X-RAY DIFFRACTION (1.87 Å)