9ARO

Crystal structure of AF9 YEATS domain in complex with acetylated at K1007 MOZ

9ARO の概要

• エントリーDOI: 10.2210/pdb9aro/pdb
• 分子名称: Protein AF-9, Acetylated Peptide from Histone acetyltransferase KAT6A, FORMIC ACID, ... (5 entities in total)
• 機能のキーワード: af9, moz, yeats, acetylation, chromatin, transcription
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 67664.26

構造登録者

Selvam, K.,Kutateladze, T.G. (登録日: 2024-02-23, 公開日: 2025-01-22, 最終更新日: 2025-04-30)

主引用文献

Becht, D.C.,Selvam, K.,Lachance, C.,Cote, V.,Li, K.,Nguyen, M.C.,Pareek, A.,Shi, X.,Wen, H.,Blanco, M.A.,Cote, J.,Kutateladze, T.G.
A multivalent engagement of ENL with MOZ.
Nat.Struct.Mol.Biol., 32:709-718, 2025

PubMed Abstract: The epigenetic cofactor ENL (eleven-nineteen-leukemia) and the acetyltransferase MOZ (monocytic leukemia zinc finger) have vital roles in transcriptional regulation and are implicated in aggressive forms of leukemia. Here, we describe the mechanistic basis for the intertwined association of ENL and MOZ. Genomic analysis shows that ENL and MOZ co-occupy active promoters and that MOZ recruits ENL to its gene targets. Structural studies reveal a multivalent assembly of ENL at the intrinsically disordered region (IDR) of MOZ. While the extraterminal (ET) domain of ENL recognizes the canonical ET-binding motif in IDR, the YEATS domains of ENL and homologous AF9 bind to a set of acetylation sites in the MOZ IDR that are generated by the acetyltransferase CBP (CREB-binding protein). Our findings suggest a multifaceted acetylation-dependent and independent coupling of ENL, MOZ and CBP/p300, which may contribute to leukemogenic activities of the ENL-MOZ assembly and chromosomal translocations of ENL, MOZ and CBP/p300.

PubMed: 39794553
DOI: 10.1038/s41594-024-01455-8

実験手法

X-RAY DIFFRACTION (2.3 Å)