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5X29

NMR structure of the SARS Coronavirus E protein pentameric ion channel

5X29 の概要
エントリーDOI10.2210/pdb5x29/pdb
関連するPDBエントリー2MM4
NMR情報BMRB: 36049
分子名称Envelope small membrane protein (1 entity in total)
機能のキーワードmembrane protein, viral protein, envelope protein, ion channel, pentamer
由来する生物種Human SARS coronavirus (SARS-CoV)
タンパク質・核酸の鎖数5
化学式量合計45017.70
構造登録者
Torres, J.,Surya, W.,Li, Y. (登録日: 2017-01-31, 公開日: 2017-06-07, 最終更新日: 2024-05-15)
主引用文献Surya, W.,Li, Y.,Torres, J.
Structural model of the SARS coronavirus E channel in LMPG micelles
Biochim. Biophys. Acta, 1860:1309-1317, 2018
Cited by
PubMed Abstract: Coronaviruses (CoV) cause common colds in humans, but are also responsible for the recent Severe Acute, and Middle East, respiratory syndromes (SARS and MERS, respectively). A promising approach for prevention are live attenuated vaccines (LAVs), some of which target the envelope (E) protein, which is a small membrane protein that forms ion channels. Unfortunately, detailed structural information is still limited for SARS-CoV E, and non-existent for other CoV E proteins. Herein, we report a structural model of a SARS-CoV E construct in LMPG micelles with, for the first time, unequivocal intermolecular NOEs. The model corresponding to the detergent-embedded region is consistent with previously obtained orientational restraints obtained in lipid bilayers and in vivo escape mutants. The C-terminal domain is mostly α-helical, and extramembrane intermolecular NOEs suggest interactions that may affect the TM channel conformation.
PubMed: 29474890
DOI: 10.1016/j.bbamem.2018.02.017
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 5x29
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2025-04-02に公開中

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