6WAU

Complex structure of PHF19

6WAU の概要

• エントリーDOI: 10.2210/pdb6wau/pdb
• 分子名称: PHD finger protein 19, Histone H3.1t peptide, UNKNOWN ATOM OR ION, ... (4 entities in total)
• 機能のキーワード: phf19, tudor, histone variant, complex, structural genomics, structural genomics consortium, sgc, gene regulation
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 48919.85

構造登録者

Dong, C.,Bountra, C.,Edwards, A.M.,Arrowsmith, C.H.,Min, J.R.,Structural Genomics Consortium (SGC) (登録日: 2020-03-26, 公開日: 2020-08-26, 最終更新日: 2023-10-18)

主引用文献

Dong, C.,Nakagawa, R.,Oyama, K.,Yamamoto, Y.,Zhang, W.,Dong, A.,Li, Y.,Yoshimura, Y.,Kamiya, H.,Nakayama, J.I.,Ueda, J.,Min, J.
Structural basis for histone variant H3tK27me3 recognition by PHF1 and PHF19.
Elife, 9:-, 2020

PubMed Abstract: The Polycomb repressive complex 2 (PRC2) is a multicomponent histone H3K27 methyltransferase complex, best known for silencing the genes during embryonic development. The Polycomb-like proteins PHF1, MTF2, and PHF19 are critical components of PRC2 by stimulating its catalytic activity in embryonic stem cells. The Tudor domains of PHF1/19 have been previously shown to be readers of H3K36me3 in vitro. However, some other studies suggest that PHF1 and PHF19 co-localize with the H3K27me3 mark but not H3K36me3 in cells. Here, we provide further evidence that PHF1 co-localizes with H3t in testis and its Tudor domain preferentially binds to H3tK27me3 over canonical H3K27me3 in vitro. Our complex structures of the Tudor domains of PHF1 and PHF19 with H3tK27me3 shed light on the molecular basis for preferential recognition of H3tK27me3 by PHF1 and PHF19 over canonical H3K27me3, implicating that H3tK27me3 might be a physiological ligand of PHF1/19.

PubMed: 32869745
DOI: 10.7554/eLife.58675

実験手法

X-RAY DIFFRACTION (1.75 Å)