3KQI

crystal structure of PHF2 PHD domain complexed with H3K4Me3 peptide

3KQI の概要

• エントリーDOI: 10.2210/pdb3kqi/pdb
• 分子名称: PHD finger protein 2, H3K4Me3 peptide, ZINC ION, ... (7 entities in total)
• 機能のキーワード: phd finger, metal-binding, zinc-finger, histone-binding, nuclear protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 10233.44

構造登録者

Wen, H.,Li, J.Z.,Song, T.,Lu, M.,Lee, M. (登録日: 2009-11-17, 公開日: 2010-02-02, 最終更新日: 2019-02-13)

主引用文献

Wen, H.,Li, J.,Song, T.,Lu, M.,Kan, P.Y.,Lee, M.G.,Sha, B.,Shi, X.
Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation.
J.Biol.Chem., 285:9322-9326, 2010

PubMed Abstract: Distinct lysine methylation marks on histones create dynamic signatures deciphered by the "effector" modules, although the underlying mechanisms remain unclear. We identified the plant homeodomain- and Jumonji C domain-containing protein PHF2 as a novel histone H3K9 demethylase. We show in biochemical and crystallographic analyses that PHF2 recognizes histone H3K4 trimethylation through its plant homeodomain finger and that this interaction is essential for PHF2 occupancy and H3K9 demethylation at rDNA promoters. Our study provides molecular insights into the mechanism by which distinct effector domains within a protein cooperatively modulate the "cross-talk" of histone modifications.

PubMed: 20129925
DOI: 10.1074/jbc.C109.097667

実験手法

X-RAY DIFFRACTION (1.78 Å)