Mechanistic Origin of Different Binding Affinities of SARS-CoV and SARS-CoV-2 Spike RBDs to Human ACE2.

ABSTRACT: The receptor-binding domain (RBD) of the SARS-CoV-2 spike protein (RBD_CoV2) has a higher binding affinity to the human receptor angiotensin-converting enzyme 2 (ACE2) than the SARS-CoV RBD (RBD_CoV). Here, we performed molecular dynamics (MD) simulations, binding free energy (BFE) calculations, and interface residue contact network (IRCN) analysis to explore the mechanistic origin of different ACE2-binding affinities of the two RBDs. The results demonstrate that, when compared to the RBD_CoV2-ACE2 complex, RBD_CoV-ACE2 features enhanced dynamicsand inter-protein positional movements and increased conformational entropy and conformational diversity. Although the inter-protein electrostatic attractive interactions are the primary

SUBMITTER: Zhang ZB 

PROVIDER: S-EPMC9032924 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature