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2XML

Crystal structure of human JMJD2C catalytic domain

2XML の概要
エントリーDOI10.2210/pdb2xml/pdb
関連するPDBエントリー2XDP
分子名称LYSINE-SPECIFIC DEMETHYLASE 4C, N-OXALYLGLYCINE, NICKEL (II) ION, ... (7 entities in total)
機能のキーワードoxidoreductase, transcription regulation, metal binding
由来する生物種HOMO SAPIENS (HUMAN)
細胞内の位置Nucleus : Q9H3R0
タンパク質・核酸の鎖数2
化学式量合計81694.37
構造登録者
主引用文献Hillringhaus, L.,Yue, W.W.,Rose, N.R.,Ng, S.S.,Gileadi, C.,Loenarz, C.,Bello, S.H.,Bray, J.E.,Schofield, C.J.,Oppermann, U.
Structural and Evolutionary Basis for the Dual Substrate Selectivity of Human Kdm4 Histone Demethylase Family.
J.Biol.Chem., 286:41616-, 2011
Cited by
PubMed Abstract: N(ε)-Methylations of histone lysine residues play critical roles in cell biology by "marking" chromatin for transcriptional activation or repression. Lysine demethylases reverse N(ε)-methylation in a sequence- and methylation-selective manner. The determinants of sequence selectivity for histone demethylases have been unclear. The human JMJD2 (KDM4) H3K9 and H3K36 demethylases can be divided into members that act on both H3K9 and H3K36 and H3K9 alone. Kinetic, crystallographic, and mutagenetic studies in vitro and in cells on KDM4A-E reveal that selectivity is determined by multiple interactions within the catalytic domain but outside the active site. Structurally informed phylogenetic analyses reveal that KDM4A-C orthologues exist in all genome-sequenced vertebrates with earlier animals containing only a single KDM4 enzyme. KDM4D orthologues only exist in eutherians (placental mammals) where they are conserved, including proposed substrate sequence-determining residues. The results will be useful for the identification of inhibitors for specific histone demethylases.
PubMed: 21914792
DOI: 10.1074/JBC.M111.283689
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.55 Å)
構造検証レポート
Validation report summary of 2xml
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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