2XL3

WDR5 IN COMPLEX WITH AN RBBP5 PEPTIDE AND HISTONE H3 PEPTIDE

2XL3 の概要

• エントリーDOI: 10.2210/pdb2xl3/pdb
• 関連するPDBエントリー: 1GUW 1U35 2WP1 2XL2
• 分子名称: WD REPEAT-CONTAINING PROTEIN 5, RETINOBLASTOMA-BINDING PROTEIN 5, HISTONE H3.1, ... (5 entities in total)
• 機能のキーワード: transcription, mll complex, h3k4 methylation, wd-40 beta-propeller
• 由来する生物種: MUS MUSCULUS (MOUSE); 詳細
• 細胞内の位置: Nucleus (By similarity): P61965 Q8BX09; Nucleus: P68433
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 78824.70

構造登録者

Odho, Z.,Southall, S.M.,Wilson, J.R. (登録日: 2010-07-19, 公開日: 2010-08-04, 最終更新日: 2023-12-20)

主引用文献

Odho, Z.,Southall, S.M.,Wilson, J.R.
Characterisation of a Novel Wdr5 Binding Site that Recruits Rbbp5 Through a Conserved Motif and Enhances Methylation of H3K4 by Mll1.
J.Biol.Chem., 285:32967-, 2010

PubMed Abstract: Histone modification is well established as a fundamental mechanism driving the regulation of transcription, replication, and DNA repair through the control of chromatin structure. Likewise, it is apparent that incorrect targeting of histone modifications contributes to misregulated gene expression and hence to developmental disorders and diseases of genomic instability such as cancer. The KMT2 family of SET domain methyltransferases, typified by mixed lineage leukemia protein-1 (MLL1), is responsible for histone H3 lysine 4 methylation, a marker of active genes. To ensure that this modification is correctly targeted, a multiprotein complex associates with the methyltransferase and directs activity. We have identified a novel interaction site on the core complex protein WD repeat protein-5 (WDR5), and we mapped the complementary site on its partner retinoblastoma-binding protein-5 (RbBP5). We have characterized this interaction by x-ray crystallography and show how it is fundamental to the assembly of the complex and to the regulation of methyltransferase activity. We show which region of RbBP5 contributes directly to mixed lineage leukemia activation, and we combine our structural and biochemical data to produce a model to show how WDR5 and RbBP5 act cooperatively to stimulate activity.

PubMed: 20716525
DOI: 10.1074/JBC.M110.159921

実験手法

X-RAY DIFFRACTION (2.7 Å)