1KNE

Chromo domain of HP1 complexed with histone H3 tail containing trimethyllysine 9

1KNE の概要

• エントリーDOI: 10.2210/pdb1kne/pdb
• 関連するPDBエントリー: 1KNA
• 分子名称: HETEROCHROMATIN PROTEIN 1, Trimethylated Histone H3 (3 entities in total)
• 機能のキーワード: chromo, hp1, histone, trimethyllysine, methyllysine, h3, chromatin, structural protein
• 由来する生物種: Drosophila melanogaster (fruit fly); 詳細
• 細胞内の位置: Nucleus: P05205; Nucleus (By similarity): P02299
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 10357.52

構造登録者

Jacobs, S.A.,Khorasanizadeh, S. (登録日: 2001-12-18, 公開日: 2002-03-20, 最終更新日: 2021-10-27)

主引用文献

Jacobs, S.A.,Khorasanizadeh, S.
Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail.
Science, 295:2080-2083, 2002

PubMed Abstract: The chromodomain of the HP1 family of proteins recognizes histone tails with specifically methylated lysines. Here, we present structural, energetic, and mutational analyses of the complex between the Drosophila HP1 chromodomain and the histone H3 tail with a methyllysine at residue 9, a modification associated with epigenetic silencing. The histone tail inserts as a beta strand, completing the beta-sandwich architecture of the chromodomain. The methylammonium group is caged by three aromatic side chains, whereas adjacent residues form discerning contacts with one face of the chromodomain. Comparison of dimethyl- and trimethyllysine-containing complexes suggests a role for cation-pi and van der Waals interactions, with trimethylation slightly improving the binding affinity.

PubMed: 11859155
DOI: 10.1126/science.1069473

実験手法

X-RAY DIFFRACTION (2.4 Å)