5XNV

Crystal structure of YEATS2 YEATS bound to H3K27ac peptide

5XNV の概要

• エントリーDOI: 10.2210/pdb5xnv/pdb
• 分子名称: YEATS domain-containing protein 2, ALA-ALA-ARG-ALY-SER-ALA-PRO-ALA, AMMONIUM ION, ... (5 entities in total)
• 機能のキーワード: epigenetics, histone reader, histone acetylation, protein complex, protein binding-peptide complex, protein binding/peptide
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus : Q9ULM3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16721.60

構造登録者

Li, H.T.,Guan, H.P.,Zhao, D. (登録日: 2017-05-24, 公開日: 2017-11-01, 最終更新日: 2024-10-16)

主引用文献

Mi, W.,Guan, H.,Lyu, J.,Zhao, D.,Xi, Y.,Jiang, S.,Andrews, F.H.,Wang, X.,Gagea, M.,Wen, H.,Tora, L.,Dent, S.Y.R.,Kutateladze, T.G.,Li, W.,Li, H.,Shi, X.
YEATS2 links histone acetylation to tumorigenesis of non-small cell lung cancer.
Nat Commun, 8:1088-1088, 2017

PubMed Abstract: Recognition of modified histones by "reader" proteins constitutes a key mechanism regulating diverse chromatin-associated processes important for normal and neoplastic development. We recently identified the YEATS domain as a novel acetyllysine-binding module; however, the functional importance of YEATS domain-containing proteins in human cancer remains largely unknown. Here, we show that the YEATS2 gene is highly amplified in human non-small cell lung cancer (NSCLC) and is required for cancer cell growth and survival. YEATS2 binds to acetylated histone H3 via its YEATS domain. The YEATS2-containing ATAC complex co-localizes with H3K27 acetylation (H3K27ac) on the promoters of actively transcribed genes. Depletion of YEATS2 or disruption of the interaction between its YEATS domain and acetylated histones reduces the ATAC complex-dependent promoter H3K9ac levels and deactivates the expression of essential genes. Taken together, our study identifies YEATS2 as a histone H3K27ac reader that regulates a transcriptional program essential for NSCLC tumorigenesis.

PubMed: 29057918
DOI: 10.1038/s41467-017-01173-4

実験手法

X-RAY DIFFRACTION (2.696 Å)