Characterization of alternate encounter assemblies of SARS-CoV-2 main protease.

ABSTRACT: The assembly of two monomeric constructs spanning segments 1-199 (MPro^1-199) and 10-306 (MPro^10-306) of SARS-CoV-2 main protease (MPro) was examined to assess the existence of a transient heterodimer intermediate in the N-terminal autoprocessing pathway of MPro model precursor. Together, they form a heterodimer population accompanied by a 13-fold increase in catalytic activity. Addition of inhibitor GC373 to the proteins increases the activity further by ∼7-fold with a 1:1 complex and higher order assemblies approaching 1:2 and 2:2 molecules of MPro^1-199 and MPro^10-306 detectable by analytical ultracentrifugation and native mass estimation by light scattering. Assemblies larger than a heterodimer (1:1) are discussed in terms of alternate pathways

SUBMITTER: Aniana A 

PROVIDER: S-EPMC11416275 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature