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1GUW

STRUCTURE OF THE CHROMODOMAIN FROM MOUSE HP1beta IN COMPLEX WITH THE LYSINE 9-METHYL HISTONE H3 N-TERMINAL PEPTIDE, NMR, 25 STRUCTURES

1GUW の概要
エントリーDOI10.2210/pdb1guw/pdb
関連するPDBエントリー1AP0 1DZ1
分子名称CHROMOBOX PROTEIN HOMOLOG 1, HISTONE H3.1 (2 entities in total)
機能のキーワードchromatin-binding, lysine methylation, heterochromatin, histone modification
由来する生物種MUS MUSCULUS (MOUSE)
詳細
タンパク質・核酸の鎖数2
化学式量合計10525.67
構造登録者
Nielsen, P.R.,Nietlispach, D.,Mott, H.R.,Callaghan, J.M.,Bannister, A.,Kouzarides, T.,Murzin, A.G.,Murzina, N.V.,Laue, E.D. (登録日: 2002-02-01, 公開日: 2002-03-12, 最終更新日: 2025-04-09)
主引用文献Nielsen, P.R.,Nietlispach, D.,Mott, H.R.,Callaghan, J.M.,Bannister, A.,Kouzarides, T.,Murzin, A.G.,Murzina, N.V.,Laue, E.D.
Structure of the Hp1 Chromodomain Bound to Histone H3 Methylated at Lysine 9
Nature, 416:103-107, 2002
Cited by
PubMed Abstract: Specific modifications to histones are essential epigenetic markers---heritable changes in gene expression that do not affect the DNA sequence. Methylation of lysine 9 in histone H3 is recognized by heterochromatin protein 1 (HP1), which directs the binding of other proteins to control chromatin structure and gene expression. Here we show that HP1 uses an induced-fit mechanism for recognition of this modification, as revealed by the structure of its chromodomain bound to a histone H3 peptide dimethylated at Nzeta of lysine 9. The binding pocket for the N-methyl groups is provided by three aromatic side chains, Tyr21, Trp42 and Phe45, which reside in two regions that become ordered on binding of the peptide. The side chain of Lys9 is almost fully extended and surrounded by residues that are conserved in many other chromodomains. The QTAR peptide sequence preceding Lys9 makes most of the additional interactions with the chromodomain, with HP1 residues Val23, Leu40, Trp42, Leu58 and Cys60 appearing to be a major determinant of specificity by binding the key buried Ala7. These findings predict which other chromodomains will bind methylated proteins and suggest a motif that they recognize.
PubMed: 11882902
DOI: 10.1038/NATURE722
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 1guw
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2026-04-22に公開中

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