Crystal structure of SARS-CoV 3C-like protease with baicalein

Jingwen Feng; Dongyang Li; Jin Zhang; Xiushan Yin; Jian Li

doi:10.1016/j.bbrc.2022.04.086

Crystal structure of SARS-CoV 3C-like protease with baicalein

Biochem Biophys Res Commun. 2022 Jun 30:611:190-194. doi: 10.1016/j.bbrc.2022.04.086. Epub 2022 Apr 22.

Authors

Jingwen Feng¹, Dongyang Li², Jin Zhang³, Xiushan Yin¹, Jian Li⁴

Affiliations

¹ Applied Biology Laboratory, College of Pharmaceutical and Biological Engineering, Shenyang University of Chemical Technology, Shenyang, 110142, China.
² Applied Biology Laboratory, College of Pharmaceutical and Biological Engineering, Shenyang University of Chemical Technology, Shenyang, 110142, China; College of Pharmaceutical Sciences, Gannan Medical University, Ganzhou, 341000, China.
³ School of Basic Medical Sciences, Nanchang University, Nanchang, 330031, China.
⁴ College of Pharmaceutical Sciences, Gannan Medical University, Ganzhou, 341000, China. Electronic address: rmsl_2040@163.com.

Abstract

The 3C-like protease (M^pro, 3CL^pro) plays a key role in the replication process in coronaviruses (CoVs). The M^pro is an essential enzyme mediates CoVs replication and is a promising target for development of antiviral drugs. Until now, baicalein has been shown the specific activity for SARS-CoV M^pro in vitro experiments. In this study, we resolved the SARS-CoV M^pro with baicalein by X-ray diffraction at 2.25 Å (PDB code 7XAX), which provided a structural basis for the research and development of baicalein as an anti-CoVs drug.

Keywords: 3C-like protease; Baicalein; SARS-CoV.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Antiviral Agents / chemistry
Antiviral Agents / pharmacology
Coronavirus 3C Proteases
Flavanones
Peptide Hydrolases
Protease Inhibitors / chemistry
SARS-CoV-2
Severe acute respiratory syndrome-related coronavirus*

Substances

Antiviral Agents
Flavanones
Protease Inhibitors
baicalein
Peptide Hydrolases
Coronavirus 3C Proteases