SARS‐CoV‐2 Mpro Dihedral Angles Reveal Allosteric Signaling

• Published in: Proteins, structure, function, and bioinformatics Vol. 93; no. 7; pp. 1281 - 1289
• Main Authors: Evans, Daniel, Sheraz, Samreen, Lau, Albert Y.
• Format: Journal Article
• Language: English
• Published: Hoboken, USA John Wiley & Sons, Inc 01.07.2025; Wiley Subscription Services, Inc
• Subjects: Allosteric properties; Allosteric Regulation; Allosteric Site; Binding Sites; Catalytic Domain; computational chemistry; coronavirus 3C proteases; Coronavirus 3C Proteases - chemistry; Coronavirus 3C Proteases - metabolism; Humans; Models, Molecular; Molecular Dynamics Simulation; Protein Binding; Protein Conformation; Proteins; SARS-CoV-2 - chemistry; SARS-CoV-2 - enzymology; SARS‐CoV‐2; Severe acute respiratory syndrome; Severe acute respiratory syndrome coronavirus 2; Signal Transduction; Therapeutic targets; protein conformation; computational chemistry; SARS‐CoV‐2; coronavirus 3C proteases; molecular dynamics simulation

ABSTRACT In allosteric proteins, identifying the pathways that signals take from allosteric ligand‐binding sites to enzyme active sites or binding pockets and interfaces remains challenging. This avenue of research is motivated by the goals of understanding particular macromolecular systems of inter...