2RVM

Solution structure of the chromodomain of HP1alpha with the phosphorylated N-terminal tail

2RVM の概要

• エントリーDOI: 10.2210/pdb2rvm/pdb
• 関連するPDBエントリー: 2RVL 2RVN
• NMR情報: BMRB: 11605
• 分子名称: Chromobox protein homolog 5 (1 entity in total)
• 機能のキーワード: chromodomain, hp1alpha, transcription
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Nucleus: Q61686
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10169.05

構造登録者

Kawaguchi, A.,Nishimura, Y. (登録日: 2015-12-18, 公開日: 2016-03-16, 最終更新日: 2024-10-30)

主引用文献

Shimojo, H.,Kawaguchi, A.,Oda, T.,Hashiguchi, N.,Omori, S.,Moritsugu, K.,Kidera, A.,Hiragami-Hamada, K.,Nakayama, J.,Sato, M.,Nishimura, Y.
Extended string-like binding of the phosphorylated HP1 alpha N-terminal tail to the lysine 9-methylated histone H3 tail
Sci Rep, 6:22527-22527, 2016

PubMed Abstract: The chromodomain of HP1α binds directly to lysine 9-methylated histone H3 (H3K9me). This interaction is enhanced by phosphorylation of serine residues in the N-terminal tail of HP1α by unknown mechanism. Here we show that phosphorylation modulates flexibility of HP1α's N-terminal tail, which strengthens the interaction with H3. NMR analysis of HP1α's chromodomain with N-terminal tail reveals that phosphorylation does not change the overall tertiary structure, but apparently reduces the tail dynamics. Small angle X-ray scattering confirms that phosphorylation contributes to extending HP1α's N-terminal tail. Systematic analysis using deletion mutants and replica exchange molecular dynamics simulations indicate that the phosphorylated serines and following acidic segment behave like an extended string and dynamically bind to H3 basic residues; without phosphorylation, the most N-terminal basic segment of HP1α inhibits interaction of the acidic segment with H3. Thus, the dynamic string-like behavior of HP1α's N-terminal tail underlies the enhancement in H3 binding due to phosphorylation.

PubMed: 26934956
DOI: 10.1038/srep22527

実験手法

SOLUTION NMR