3EMH

Structural basis of WDR5-MLL interaction

3EMH の概要

• エントリーDOI: 10.2210/pdb3emh/pdb
• 分子名称: WD repeat-containing protein 5, Mixed-lineage leukemia protein 1, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: chromatin, histone, wd40 repeat, nucleus, phosphoprotein, wd repeat, zinc-finger, gene regulation
• 由来する生物種: Homo sapiens; 詳細
• 細胞内の位置: Nucleus: P61964
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36612.42

構造登録者

Song, J.J.,Kingston, R.E. (登録日: 2008-09-24, 公開日: 2008-10-07, 最終更新日: 2023-09-06)

主引用文献

Song, J.J.,Kingston, R.E.
WDR5 Interacts with Mixed Lineage Leukemia (MLL) Protein via the Histone H3-binding Pocket.
J.Biol.Chem., 283:35258-35264, 2008

PubMed Abstract: WDR5 is a component of the mixed lineage leukemia (MLL) complex, which methylates lysine 4 of histone H3, and was identified as a methylated Lys-4 histone H3-binding protein. Here, we present a crystal structure of WDR5 bound to an MLL peptide. Surprisingly, we find that WDR5 utilizes the same pocket shown to bind histone H3 for this MLL interaction. Furthermore, the WDR5-MLL interaction is disrupted preferentially by mono- and di-methylated Lys-4 histone H3 over unmodified and tri-methylated Lys-4 histone H3. These data implicate a delicate interplay between the effector, WDR5, the catalytic subunit, MLL, and the substrate, histone H3, of the MLL complex. We suggest that the activity of the MLL complex might be regulated through this interplay.

PubMed: 18840606
DOI: 10.1074/jbc.M806900200

実験手法

X-RAY DIFFRACTION (1.37 Å)