5VNA

Crystal structure of human YEATS domain

5VNA の概要

• エントリーDOI: 10.2210/pdb5vna/pdb
• 関連するPDBエントリー: 5VNA
• 分子名称: YEATS domain-containing protein 4, SULFATE ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: histone reader, yeats domain, transcription
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 70479.77

構造登録者

Cho, H.J.,Cierpicki, T. (登録日: 2017-04-29, 公開日: 2018-09-05, 最終更新日: 2023-10-04)

主引用文献

Cho, H.J.,Li, H.,Linhares, B.M.,Kim, E.,Ndoj, J.,Miao, H.,Grembecka, J.,Cierpicki, T.
GAS41 Recognizes Diacetylated Histone H3 through a Bivalent Binding Mode.
ACS Chem. Biol., 13:2739-2746, 2018

PubMed Abstract: GAS41 is a chromatin-associated protein that belongs to the YEATS family and is involved in the recognition of acetyl-lysine in histone proteins. A unique feature of GAS41 is the presence of a C-terminal coiled-coil domain, which is responsible for protein dimerization. Here, we characterized the specificity of the GAS41 YEATS domain and found that it preferentially binds to acetylated H3K18 and H3K27 peptides. Interestingly, we found that full-length, dimeric GAS41 binds to diacetylated H3 peptides with an enhanced affinity when compared to those for monoacetylated peptides, through a bivalent binding mode. We determined the crystal structure of the GAS41 YEATS domain with H3K23acK27ac to visualize the molecular basis of diacetylated histone binding. Our results suggest a unique binding mode in which full-length GAS41 is a reader of diacetylated histones.

PubMed: 30071723
DOI: 10.1021/acschembio.8b00674

実験手法

X-RAY DIFFRACTION (2.1 Å)