5JJY

Crystal structure of SETD2 bound to histone H3.3 K36M peptide

5JJY の概要

• エントリーDOI: 10.2210/pdb5jjy/pdb
• 関連するPDBエントリー: 5JLB 5JLE
• 分子名称: Histone-lysine N-methyltransferase SETD2, Histone H3.3, ZINC ION, ... (6 entities in total)
• 機能のキーワード: set domain, transferase
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus : Q9BYW2 P84243
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34474.44

構造登録者

Yang, S.,Zheng, X.,Li, H. (登録日: 2016-04-25, 公開日: 2016-11-02, 最終更新日: 2024-04-03)

主引用文献

Yang, S.,Zheng, X.,Lu, C.,Li, G.M.,Allis, C.D.,Li, H.
Molecular basis for oncohistone H3 recognition by SETD2 methyltransferase
Genes Dev., 30:1611-1616, 2016

PubMed Abstract: High-frequency point mutations of genes encoding histones have been identified recently as novel drivers in a number of tumors. Specifically, the H3K36M/I mutations were shown to be oncogenic in chondroblastomas and undifferentiated sarcomas by inhibiting H3K36 methyltransferases, including SETD2. Here we report the crystal structures of the SETD2 catalytic domain bound to H3K36M or H3K36I peptides with SAH (S-adenosylhomocysteine). In the complex structure, the catalytic domain adopts an open conformation, with the K36M/I peptide snuggly positioned in a newly formed substrate channel. Our structural and biochemical data reveal the molecular basis underying oncohistone recognition by and inhibition of SETD2.

PubMed: 27474439
DOI: 10.1101/gad.284323.116

実験手法

X-RAY DIFFRACTION (2.053 Å)