4O42

Tandem chromodomains of human CHD1 in complex with influenza NS1 C-terminal tail dimethylated at K229

4O42 の概要

• エントリーDOI: 10.2210/pdb4o42/pdb
• 分子名称: Chromodomain-helicase-DNA-binding protein 1, Nonstructural protein 1, UNKNOWN ATOM OR ION, ... (5 entities in total)
• 機能のキーワード: viral, chromodomain, structural genomics, structural genomics consortium, sgc, dna binding protein-viral protein complex, dna binding protein/viral protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: O14646; Host nucleus: Q38SQ2
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24853.77

構造登録者

Qin, S.,Xu, C.,Tempel, W.,Arrowsmith, C.H.,Bountra, C.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (登録日: 2013-12-18, 公開日: 2014-04-16, 最終更新日: 2023-09-20)

主引用文献

Qin, S.,Liu, Y.,Tempel, W.,Eram, M.S.,Bian, C.,Liu, K.,Senisterra, G.,Crombet, L.,Vedadi, M.,Min, J.
Structural basis for histone mimicry and hijacking of host proteins by influenza virus protein NS1.
Nat Commun, 5:3952-3952, 2014

PubMed Abstract: Pathogens can interfere with vital biological processes of their host by mimicking host proteins. The NS1 protein of the influenza A H3N2 subtype possesses a histone H3K4-like sequence at its carboxyl terminus and has been reported to use this mimic to hijack host proteins. However, this mimic lacks a free N-terminus that is essential for binding to many known H3K4 readers. Here we show that the double chromodomains of CHD1 adopt an 'open pocket' to interact with the free N-terminal amine of H3K4, and the open pocket permits the NS1 mimic to bind in a distinct conformation. We also explored the possibility that NS1 hijacks other cellular proteins and found that the NS1 mimic has access to only a subset of chromatin-associated factors, such as WDR5. Moreover, methylation of the NS1 mimic can not be reversed by the H3K4 demethylase LSD1. Overall, we thus conclude that the NS1 mimic is an imperfect histone mimic.

PubMed: 24853335
DOI: 10.1038/ncomms4952

実験手法

X-RAY DIFFRACTION (1.87 Å)