The Conformational Space of the SARS-CoV‑2 Main Protease Active Site Loops Is Determined by Ligand Binding and Interprotomer Allostery

The main protease (M<sup>pro</sup>) of SARS-CoV-2 is essential for viral replication and is, therefore, an important drug target. Here, we investigate two flexible loops in M<sup>pro</sup> that play a role in catalysis. Using all-atom molecular dynamics simulations, we analyz...

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Bibliographic Details
Main Author:	Ethan Lee (2137) (author)
Other Authors:	Sarah Rauscher (1285638) (author)
Published:	2024
Subjects:	Biophysics Biochemistry Pharmacology Infectious Diseases Computational Biology Chemical Sciences not elsewhere classified Physical Sciences not elsewhere classified Information Systems not elsewhere classified two active sites prime drug target important drug target allosteric hotspot involving partly open ), pro </ sup apo protomer ’ apo state adopt open one protomer bound protomer viral replication taken together structural propensity structural ensemble main protease ligand binding interprotomer allostery crystal structures critical region conformational space comprises part close proximity catalytic residues bound state binding pocket also affecting
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The Conformational Space of the SARS-CoV‑2 Main Protease Active Site Loops Is Determined by Ligand Binding and Interprotomer Allostery

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