Inhibitor binding influences the protonation states of histidines in SARS-CoV-2 main protease
Ànna Pavlova, Diane L. Lynch, Isabella Daidone, Laura Zanetti‐Polzi, Micholas Dean Smith, Chris Chipot, Daniel W. Kneller, Andrey Kovalevsky, Leighton Coates, Andrei A. Golosov, Callum J. Dickson, Camilo Velez‐Vega, José S. Duca, Josh V. Vermaas, Yui Tik Pang, Atanu Acharya, Jerry M. Parks, Jeremy C. Smith, James C. Gumbart
Abstract
The main protease (M pro ) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an attractive target for antiviral therapeutics.
Topics & Concepts
ProtonationChemistryProteaseSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)Coronavirus disease 2019 (COVID-19)2019-20 coronavirus outbreakStereochemistryBiochemistryVirologyCombinatorial chemistryEnzymeBiologyOrganic chemistryMedicineOutbreakPathologyDiseaseInfectious disease (medical specialty)IonComputational Drug Discovery MethodsSARS-CoV-2 and COVID-19 ResearchProtein Structure and Dynamics