2MNZ

NMR Structure of KDM5B PHD1 finger in complex with H3K4me0(1-10aa)

2MNZ の概要

• エントリーDOI: 10.2210/pdb2mnz/pdb
• 関連するPDBエントリー: 1MNY
• NMR情報: BMRB: 19914
• 分子名称: Lysine-specific demethylase 5B, H3K4me0, ZINC ION (3 entities in total)
• 機能のキーワード: kdm5b, phd1, h3k4, demethylase, repression, oxidoreductase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: Q9UGL1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 7414.15

構造登録者

Zhang, Y.,Yang, H.R.,Guo, X.,Rong, N.Y.,Song, Y.J.,Xu, Y.W.,Lan, W.X.,Xu, Y.H.,Cao, C. (登録日: 2014-04-16, 公開日: 2014-08-06, 最終更新日: 2024-05-15)

主引用文献

Zhang, Y.,Yang, H.,Guo, X.,Rong, N.,Song, Y.,Xu, Y.,Lan, W.,Zhang, X.,Liu, M.,Xu, Y.,Cao, C.
The PHD1 finger of KDM5B recognizes unmodified H3K4 during the demethylation of histone H3K4me2/3 by KDM5B.
Protein Cell, 5:837-850, 2014

PubMed Abstract: KDM5B is a histone H3K4me2/3 demethylase. The PHD1 domain of KDM5B is critical for demethylation, but the mechanism underlying the action of this domain is unclear. In this paper, we observed that PHD1KDM5B interacts with unmethylated H3K4me0. Our NMR structure of PHD1KDM5B in complex with H3K4me0 revealed that the binding mode is slightly different from that of other reported PHD fingers. The disruption of this interaction by double mutations on the residues in the interface (L325A/D328A) decreases the H3K4me2/3 demethylation activity of KDM5B in cells by approximately 50% and increases the transcriptional repression of tumor suppressor genes by approximately twofold. These findings imply that PHD1KDM5B may help maintain KDM5B at target genes to mediate the demethylation activities of KDM5B.

PubMed: 24952722
DOI: 10.1007/s13238-014-0078-4

実験手法

SOLUTION NMR