Activity profiling and crystal structures of inhibitor-bound SARS-CoV-2 papain-like protease: A framework for anti–COVID-19 drug design

• DOI: 10.1126/sciadv.abd4596
• Publication Date: 2020-10-16T23:19:01Z
• Authors: Wioletta Rut; Zongyang Lv; Mikolaj Zmudzinski; Stephanie Patchett; Digant Nayak; Scott J. Snipas; Farid El Oualid; Tony T. Huang; Miklos Bekes; Marcin Drag; Shaun K. Olsen
• Keywords: 0301 basic medicine; Pneumonia, Viral; Molecular Dynamics Simulation; Crystallography, X-Ray; Substrate Specificity; Betacoronavirus; 03 medical and health sciences; Catalytic Domain; Humans; Protease Inhibitors; Amino Acid Sequence; Pandemics; Research Articles; Coronavirus 3C Proteases; Multidisciplinary; Binding Sites; SARS-CoV-2; COVID-19; Recombinant Proteins; 3. Good health; Cysteine Endopeptidases; Kinetics; Drug Design; Coronavirus Infections; Oligopeptides

A multidisciplinary approach yields novel inhibitors and reveals substrate specificity, structure, and mechanisms of CoV-2 PLpro.