The COVID-19 disease caused by the SARS-CoV-2 coronavirus has become a pandemic health crisis. An attractive target for antiviral inhibitors is the main protease 3CL M pro due to its essential role in processing the polyproteins translated from viral RNA. Here we report the room temperature X-ray structure of unliganded SARS-CoV-2 3CL M pro , revealing the ligand-free structure of the active site and the conformation of the catalytic site cavity at near-physiological temperature. Comparison with previously reported low-temperature ligand-free and inhibitor-bound structures suggest that the room temperature structure may provide more relevant information at physiological temperatures for aiding in molecular docking studies. The SARS-CoV-2 3CL main protease (3CL M pro ) is a chymotrypsin-like protease that facilitates the production of non-structural proteins, which are essential for viral replication and is therefore of great interest as a drug target. Here, the authors present the 2.30 Å room temperature crystal structure of ligand-free 3CL M pro and compare it with the earlier determined low-temperature ligand-free and inhibitor-bound crystal structures.
【저자키워드】 X-ray crystallography, Target validation, Hydrolases, 【초록키워드】 Structure, SARS-CoV-2, coronavirus, pandemic, protease, non-structural proteins, COVID-19 disease, X-ray, Health, viral replication, drug target, temperature, Viral RNA, information, 3CL, crystal structures, M pro, physiological temperature, catalytic site, molecular docking studies, polyprotein, caused, reported, facilitate, translated, antiviral inhibitor, the SARS-CoV-2, unliganded, 【제목키워드】 SARS-CoV-2, temperature, 3CL, M pro, plasticity,