5X5C

Prefusion structure of MERS-CoV spike glycoprotein, conformation 1

5X5C の概要

• エントリーDOI: 10.2210/pdb5x5c/pdb
• 関連するPDBエントリー: 5X59
• EMDBエントリー: 6706
• 分子名称: S protein (1 entity in total)
• 機能のキーワード: mers-cov, spike glycoprotein, prefusion, single particle, viral protein
• 由来する生物種: Middle East respiratory syndrome coronavirus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 437568.61

構造登録者

Yuan, Y.,Cao, D.,Zhang, Y.,Ma, J.,Qi, J.,Wang, Q.,Lu, G.,Wu, Y.,Yan, J.,Shi, Y.,Zhang, X.,Gao, G.F. (登録日: 2017-02-15, 公開日: 2017-05-03, 最終更新日: 2024-10-16)

主引用文献

Yuan, Y.,Cao, D.,Zhang, Y.,Ma, J.,Qi, J.,Wang, Q.,Lu, G.,Wu, Y.,Yan, J.,Shi, Y.,Zhang, X.,Gao, G.F.
Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains
Nat Commun, 8:15092-15092, 2017

PubMed Abstract: The envelope spike (S) proteins of MERS-CoV and SARS-CoV determine the virus host tropism and entry into host cells, and constitute a promising target for the development of prophylactics and therapeutics. Here, we present high-resolution structures of the trimeric MERS-CoV and SARS-CoV S proteins in its pre-fusion conformation by single particle cryo-electron microscopy. The overall structures resemble that from other coronaviruses including HKU1, MHV and NL63 reported recently, with the exception of the receptor binding domain (RBD). We captured two states of the RBD with receptor binding region either buried (lying state) or exposed (standing state), demonstrating an inherently flexible RBD readily recognized by the receptor. Further sequence conservation analysis of six human-infecting coronaviruses revealed that the fusion peptide, HR1 region and the central helix are potential targets for eliciting broadly neutralizing antibodies.

PubMed: 28393837
DOI: 10.1038/ncomms15092

実験手法

ELECTRON MICROSCOPY (4.1 Å)