Elucidation of interactions regulating conformational stability and dynamics of SARS-CoV-2 S-protein.

ABSTRACT: The ongoing COVID-19 pandemic caused by the new coronavirus, SARS-CoV-2, calls for urgent developments of vaccines and antiviral drugs. The spike protein of SARS-CoV-2 (S-protein), which consists of trimeric polypeptide chains with glycosylated residues on the surface, triggers the virus entry into a host cell. Extensive structural and functional studies on this protein have rapidly advanced our understanding of the S-protein structure at atomic resolutions, although most of these structural studies overlook the effect of glycans attached to the S-protein on the conformational stability and functional motions between the inactive down and active up forms. Here, we performed all-atom molecular dynamics simulations of both down and up forms of a fully glycosylated S-protein in solution as we

SUBMITTER: Mori T 

PROVIDER: S-EPMC7825899 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature