Structural plasticity of SARS-CoV-2 3CL Mpro active site cavity revealed by room temperature X-ray crystallography

Autor: Daniel W. Kneller, Gwyndalyn Phillips, Hugh M. O’Neill, Robert Jedrzejczak, Lucy Stols, Paul Langan, Andrzej Joachimiak, Leighton Coates, Andrey Kovalevsky
Jazyk: angličtina
Rok vydání: 2020
Předmět:
Zdroj: Nature Communications, Vol 11, Iss 1, Pp 1-6 (2020)
Druh dokumentu: article
ISSN: 2041-1723
DOI: 10.1038/s41467-020-16954-7
Popis: The SARS-CoV-2 3CL main protease (3CL Mpro) 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 Mpro and compare it with the earlier determined low-temperature ligand-free and inhibitor-bound crystal structures.
Databáze: Directory of Open Access Journals