2LBM

Solution structure of the ADD domain of ATRX complexed with histone tail H3 1-15 K9me3

2LBM の概要

• エントリーDOI: 10.2210/pdb2lbm/pdb
• NMR情報: BMRB: 17569
• 分子名称: Transcriptional regulator ATRX, histone tail H3 K9me3, ZINC ION (3 entities in total)
• 機能のキーワード: histone tail, metal binding protein-structural protein complex, metal binding protein/structural protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: P46100
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18078.71

構造登録者

Eustermann, S.,Yang, J.,Neuhaus, D. (登録日: 2011-04-08, 公開日: 2011-06-29, 最終更新日: 2025-03-26)

主引用文献

Eustermann, S.,Yang, J.,Law, M.J.,Amos, R.,Chapman, L.M.,Jelinska, C.,Garrick, D.,Clynes, D.,Gibbons, R.J.,Rhodes, D.,Higgs, D.R.,Neuhaus, D.
Combinatorial readout of histone H3 modifications specifies localization of ATRX to heterochromatin
Nat.Struct.Mol.Biol., 2011

PubMed Abstract: Accurate read-out of chromatin modifications is essential for eukaryotic life. Mutations in the gene encoding X-linked ATRX protein cause a mental-retardation syndrome, whereas wild-type ATRX protein targets pericentric and telomeric heterochromatin for deposition of the histone variant H3.3 by means of a largely unknown mechanism. Here we show that the ADD domain of ATRX, in which most syndrome-causing mutations occur, engages the N-terminal tail of histone H3 through two rigidly oriented binding pockets, one for unmodified Lys4 and the other for di- or trimethylated Lys9. In vivo experiments show this combinatorial readout is required for ATRX localization, with recruitment enhanced by a third interaction through heterochromatin protein-1 (HP1) that also recognizes trimethylated Lys9. The cooperation of ATRX ADD domain and HP1 in chromatin recruitment results in a tripartite interaction that may span neighboring nucleosomes and illustrates how the 'histone-code' is interpreted by a combination of multivalent effector-chromatin interactions.

PubMed: 21666677
DOI: 10.1038/nsmb.2070

実験手法

SOLUTION NMR