4HCZ

PHF1 Tudor in complex with H3K36me3

4HCZ の概要

• エントリーDOI: 10.2210/pdb4hcz/pdb
• 分子名称: PHD finger protein 1, H3L-like histone (3 entities in total)
• 機能のキーワード: protein-peptide complex, tudor, histone binding, h3k36me3, na, nucleus, transcription
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: O43189
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 15471.79

構造登録者

Musselman, C.A.,Roy, S.,Nunez, J.,Kutateladze, T.G. (登録日: 2012-10-01, 公開日: 2012-11-14, 最終更新日: 2023-09-20)

主引用文献

Musselman, C.A.,Avvakumov, N.,Watanabe, R.,Abraham, C.G.,Lalonde, M.E.,Hong, Z.,Allen, C.,Roy, S.,Nunez, J.K.,Nickoloff, J.,Kulesza, C.A.,Yasui, A.,Cote, J.,Kutateladze, T.G.
Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1.
Nat.Struct.Mol.Biol., 19:1266-1272, 2012

PubMed Abstract: The PHD finger protein 1 (PHF1) is essential in epigenetic regulation and genome maintenance. Here we show that the Tudor domain of human PHF1 binds to histone H3 trimethylated at Lys36 (H3K36me3). We report a 1.9-Å resolution crystal structure of the Tudor domain in complex with H3K36me3 and describe the molecular mechanism of H3K36me3 recognition using NMR. Binding of PHF1 to H3K36me3 inhibits the ability of the Polycomb PRC2 complex to methylate Lys27 of histone H3 in vitro and in vivo. Laser microirradiation data show that PHF1 is transiently recruited to DNA double-strand breaks, and PHF1 mutants impaired in the H3K36me3 interaction exhibit reduced retention at double-strand break sites. Together, our findings suggest that PHF1 can mediate deposition of the repressive H3K27me3 mark and acts as a cofactor in early DNA-damage response.

PubMed: 23142980
DOI: 10.1038/nsmb.2435

実験手法

X-RAY DIFFRACTION (1.85 Å)