5X29
NMR structure of the SARS Coronavirus E protein pentameric ion channel
5X29 の概要
エントリーDOI | 10.2210/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 | |
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: 29474890DOI: 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
検証レポート(詳細版)
をダウンロード
