7KIP

A 3.4 Angstrom cryo-EM structure of the human coronavirus spike trimer computationally derived from vitrified NL63 virus particles

これはPDB形式変換不可エントリーです。

7KIP の概要

• エントリーDOI: 10.2210/pdb7kip/pdb
• EMDBエントリー: 22889
• 分子名称: Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total)
• 機能のキーワード: nl63, in situ, spike trimer, glycosylation sites, single particle cryo-em, viral protein
• 由来する生物種: Human coronavirus NL63 (HCoV-NL63)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 493459.55

構造登録者

Zhang, K.,Li, S.,Pintilie, G.,Chmielewski, D.,Schmid, M.,Simmons, G.,Jin, J.,Chiu, W. (登録日: 2020-10-24, 公開日: 2020-11-11, 最終更新日: 2024-10-23)

主引用文献

Zhang, K.,Li, S.,Pintilie, G.,Chmielewski, D.,Schmid, M.F.,Simmons, G.,Jin, J.,Chiu, W.
A 3.4- angstrom cryo-EM structure of the human coronavirus spike trimer computationally derived from vitrified NL63 virus particles.
Biorxiv, 2020

PubMed Abstract: Human coronavirus NL63 (HCoV-NL63) is an enveloped pathogen of the family that spreads worldwide and causes up to 10% of all annual respiratory diseases. HCoV-NL63 is typically associated with mild upper respiratory symptoms in children, elderly and immunocompromised individuals. It has also been shown to cause severe lower respiratory illness. NL63 shares ACE2 as a receptor for viral entry with SARS-CoV and SARS-CoV-2. Here we present the structure of HCoV-NL63 spike (S) trimer at 3.4-Å resolution by single-particle cryo-EM imaging of vitrified virions without chemical fixative. It is structurally homologous to that obtained previously from the biochemically purified ectodomain of HCoV-NL63 S trimer, which displays a 3-fold symmetric trimer in a single conformation. In addition to previously proposed and observed glycosylation sites, our map shows density at other amino acid positions as well as differences in glycan structures. The domain arrangement within a protomer is strikingly different from that of the SARS-CoV-2 S and may explain their different requirements for activating binding to the receptor. This structure provides the basis for future studies of spike proteins with receptors, antibodies, or drugs, in the native state of the coronavirus particles.

PubMed: 32817943
DOI: 10.1101/2020.08.11.245696

実験手法

ELECTRON MICROSCOPY (3.39 Å)