2H6N

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

2H6N の概要

• エントリーDOI: 10.2210/pdb2h6n/pdb
• 関連するPDBエントリー: 2CNX 2CO0 2H68 2H6K 2H6Q
• 分子名称: WD-repeat protein 5, Histone H3 K4-Me2 9-residue peptide (3 entities in total)
• 機能のキーワード: wd40 wd-repeat histone modification mll set chromatin, gene regulation
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: P61964
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 70788.43

構造登録者

Ruthenburg, A.J.,Wang, W.-K.,Graybosch, D.M.,Li, H.,Allis, C.D.,Patel, D.J.,Verdine, G.L. (登録日: 2006-05-31, 公開日: 2006-07-04, 最終更新日: 2023-08-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.5 Å)