The inherent flexibility of receptor binding domains in SARS-CoV-2 spike protein.

ABSTRACT: Spike (S) protein is the primary antigenic target for neutralization and vaccine development for the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). It decorates the virus surface and undergoes large motions of its receptor binding domains (RBDs) to enter the host cell. Here, we observe Down, one-Up, one-Open, and two-Up-like structures in enhanced molecular dynamics simulations, and characterize the transition pathways via inter-domain interactions. Transient salt-bridges between RBD_A and RBD_C and the interaction with glycan at N343_B support RBD_A motions from Down to one-Up. Reduced interactions between RBD_A and RBD_B in one-Up induce RBD_B motions toward two-Up. The simulations overall agree with cry

SUBMITTER: Dokainish HM 

PROVIDER: S-EPMC8963885 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature