Docking and molecular dynamics studies of human ezrin protein with a modelled SARS-CoV-2 endodomain and their interaction with potential invasion inhibitors.

ABSTRACT: Human ezrin protein interacts with SARS-CoV S endodomain and restricts virus fusion, entry, and early events of infection. In general, their binding strength and their structural stability determines their successful entry into the host cells. However, the binding affinity of these two endodomains with the ezrin protein has been elusive due to a paucity of knowledge on the 3D structure. This study modelled the endodomains of both SARS-CoV-1 and SARS-CoV-2 and then docked these models with human ezrin protein. This study establishes that the modelled endodomains of both SARS-CoV-1 and SARS-Cov-2 consisted of three disulphide bridges for self-stabilization. Protein-protein docking listed four salt bridges with a higher buried surface area between ezrin-SARS-CoV-1 endodomain compared to that

SUBMITTER: Chellasamy SK 

PROVIDER: S-EPMC9364929 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature