2QQS

JMJD2A tandem tudor domains in complex with a trimethylated histone H4-K20 peptide

2QQS の概要

• エントリーDOI: 10.2210/pdb2qqs/pdb
• 関連するPDBエントリー: 2QQR
• 分子名称: JmjC domain-containing histone demethylation protein 3A, METHYLATED HISTONE H4 PEPTIDE (3 entities in total)
• 機能のキーワード: histone lysine demethylase, metal binding protein, protein-methylated peptide complex, chromatin regulator, dioxygenase, host-virus interaction, iron, metal-binding, nucleus, oxidoreductase, phosphorylation, polymorphism, transcription, transcription regulation, zinc, zinc-finger
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: O75164
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 29650.96

構造登録者

Lee, J.,Botuyan, M.V.,Mer, G. (登録日: 2007-07-26, 公開日: 2007-12-11, 最終更新日: 2023-08-30)

主引用文献

Lee, J.,Thompson, J.R.,Botuyan, M.V.,Mer, G.
Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor.
Nat.Struct.Mol.Biol., 15:109-111, 2008

PubMed Abstract: The lysine demethylase JMJD2A has the unique property of binding trimethylated peptides from two different histone sequences (H3K4me3 and H4K20me3) through its tudor domains. Here we show using X-ray crystallography and calorimetry that H3K4me3 and H4K20me3, which are recognized with similar affinities by JMJD2A, adopt radically different binding modes, to the extent that we were able to design single point mutations in JMJD2A that inhibited the recognition of H3K4me3 but not H4K20me3 and vice versa.

PubMed: 18084306
DOI: 10.1038/nsmb1326

実験手法

X-RAY DIFFRACTION (2.82 Å)