7VFA

the complex of SARS-CoV2 3CL and NB1A2

7VFA の概要

• エントリーDOI: 10.2210/pdb7vfa/pdb
• 分子名称: NB1A2, 3C-like proteinase, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: sars-cov2, 3cl, nanobody, viral protein, viral protein-immune system complex, viral protein/immune system
• 由来する生物種: Camelus bactrianus; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 50227.00

構造登録者

Sun, Z.C.,Wang, L.,Geng, Y. (登録日: 2021-09-11, 公開日: 2022-03-30, 最終更新日: 2024-10-30)

主引用文献

Sun, Z.,Wang, L.,Li, X.,Fan, C.,Xu, J.,Shi, Z.,Qiao, H.,Lan, Z.,Zhang, X.,Li, L.,Zhou, X.,Geng, Y.
An extended conformation of SARS-CoV-2 main protease reveals allosteric targets.
Proc.Natl.Acad.Sci.USA, 119:-, 2022

PubMed Abstract: SignificanceThe coronavirus main protease (M) is required for viral replication. Here, we obtained the extended conformation of the native monomer of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) M by trapping it with nanobodies and found that the catalytic domain and the helix domain dissociate, revealing allosteric targets. Another monomeric state is termed compact conformation and is similar to one protomer of the dimeric form. We designed a Nanoluc Binary Techonology (NanoBiT)-based high-throughput allosteric inhibitor assay based on structural conformational change. Our results provide insight into the maturation, dimerization, and catalysis of the coronavirus M and pave a way to develop an anticoronaviral drug through targeting the maturation process to inhibit the autocleavage of M.

PubMed: 35324337
DOI: 10.1073/pnas.2120913119

実験手法

X-RAY DIFFRACTION (1.75 Å)