7VFA

the complex of SARS-CoV2 3CL and NB1A2

Summary for 7VFA

• Entry DOI: 10.2210/pdb7vfa/pdb
• Descriptor: NB1A2, 3C-like proteinase, SULFATE ION, ... (4 entities in total)
• Functional Keywords: sars-cov2, 3cl, nanobody, viral protein, viral protein-immune system complex, viral protein/immune system
• Biological source: Camelus bactrianus; More
• Total number of polymer chains: 2
• Total formula weight: 50227.00

Authors

Sun, Z.C.,Wang, L.,Geng, Y. (deposition date: 2021-09-11, release date: 2022-03-30, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.75 Å)