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7WVN

SARS-CoV-2 Omicron S-open

7WVN の概要
エントリーDOI10.2210/pdb7wvn/pdb
EMDBエントリー32854
分子名称Spike glycoprotein (1 entity in total)
機能のキーワードsars-cov-2, coronavirus, omicron variant, s-open, spike protein, viral protein
由来する生物種Severe acute respiratory syndrome coronavirus
タンパク質・核酸の鎖数3
化学式量合計420643.88
構造登録者
Li, J.W.,Cong, Y. (登録日: 2022-02-10, 公開日: 2022-03-02, 最終更新日: 2025-06-25)
主引用文献Hong, Q.,Han, W.,Li, J.,Xu, S.,Wang, Y.,Xu, C.,Li, Z.,Wang, Y.,Zhang, C.,Huang, Z.,Cong, Y.
Molecular basis of receptor binding and antibody neutralization of Omicron.
Nature, 604:546-552, 2022
Cited by
PubMed Abstract: The SARS-CoV-2 Omicron variant exhibits striking immune evasion and is spreading rapidly worldwide. Understanding the structural basis of the high transmissibility and enhanced immune evasion of Omicron is of high importance. Here, using cryo-electron microscopy, we present both the closed and the open states of the Omicron spike (S) protein, which appear more compact than the counterparts of the G614 strain, potentially related to enhanced inter-protomer and S1-S2 interactions induced by Omicron residue substitution. The closed state showing dominant population may indicate a conformational masking mechanism for the immune evasion of Omicron. Moreover, we captured three states for the Omicron S-ACE2 complex, revealing that the substitutions on the Omicron RBM result in new salt bridges and hydrogen bonds, more favourable electrostatic surface properties, and an overall strengthened S-ACE2 interaction, in line with the observed higher ACE2 affinity of Omicron S than of G614. Furthermore, we determined the structures of Omicron S in complex with the Fab of S3H3, an antibody that is able to cross-neutralize major variants of concern including Omicron, elucidating the structural basis for S3H3-mediated broad-spectrum neutralization. Our findings shed light on the receptor engagement and antibody neutralization or evasion of Omicron and may also inform the design of broadly effective vaccines against SARS-CoV-2.
PubMed: 35228716
DOI: 10.1038/s41586-022-04581-9
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.4 Å)
構造検証レポート
Validation report summary of 7wvn
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2026-04-22に公開中

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