8XUY

Structure of SARS-CoV-2 BA.2.86 spike glycoprotein in complex with ACE2 (2-up state)

これはPDB形式変換不可エントリーです。

8XUY の概要

• エントリーDOI: 10.2210/pdb8xuy/pdb
• EMDBエントリー: 38686
• 分子名称: Spike glycoprotein, Processed angiotensin-converting enzyme 2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: spike protein, glycoprotein, virus, viral protein, viral protein-protein binding complex, viral protein/protein binding
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV,SARS-CoV-2); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 568608.88

構造登録者

Yajima, H.,Anraku, Y.,Kita, S.,Kimura, K.,Maenaka, K.,Hashiguchi, T. (登録日: 2024-01-14, 公開日: 2024-10-09, 最終更新日: 2024-10-23)

主引用文献

Yajima, H.,Anraku, Y.,Kaku, Y.,Kimura, K.T.,Plianchaisuk, A.,Okumura, K.,Nakada-Nakura, Y.,Atarashi, Y.,Hemmi, T.,Kuroda, D.,Takahashi, Y.,Kita, S.,Sasaki, J.,Sumita, H.,Ito, J.,Maenaka, K.,Sato, K.,Hashiguchi, T.
Structural basis for receptor-binding domain mobility of the spike in SARS-CoV-2 BA.2.86 and JN.1.
Nat Commun, 15:8574-8574, 2024

PubMed Abstract: Since 2019, SARS-CoV-2 has undergone mutations, resulting in pandemic and epidemic waves. The SARS-CoV-2 spike protein, crucial for cellular entry, binds to the ACE2 receptor exclusively when its receptor-binding domain (RBD) adopts the up-conformation. However, whether ACE2 also interacts with the RBD in the down-conformation to facilitate the conformational shift to RBD-up remains unclear. Herein, we present the structures of the BA.2.86 and the JN.1 spike proteins bound to ACE2. Notably, we successfully observed the ACE2-bound down-RBD, indicating an intermediate structure before the RBD-up conformation. The wider and mobile angle of RBDs in the up-state provides space for ACE2 to interact with the down-RBD, facilitating the transition to the RBD-up state. The K356T, but not N354-linked glycan, contributes to both of infectivity and neutralizing-antibody evasion in BA.2.86. These structural insights the spike-protein dynamics would help understand the mechanisms underlying SARS-CoV-2 infection and its neutralization.

PubMed: 39375326
DOI: 10.1038/s41467-024-52808-2

実験手法

ELECTRON MICROSCOPY (3.14 Å)