In silico identification of RBD subdomain of spike protein from Pro³²²-Thr⁵⁸¹ for applications in vaccine development against SARS-CoV2.

ABSTRACT: The three-dimensional hybrid structures of coronavirus spike proteins including the C-terminal sequence and receptor binding motif (RBM) was remodeled and energy minimized. Further, protein-protein docking show that Receptor Binding Domain (RBD) of SARS-CoV 2 Lys⁴⁵⁷-Pro⁴⁹⁰ bind on the surface of ACE2 receptor near N-terminal helices to form host-pathogen attachment. In this binding interface, SARS-CoV 2 shows a tight network of hydrogen bonds than other spike proteins from BtRsRaTG13-CoV, SARS-CoV, BtRsBeta-CoV, BtRsCoV-related, Pangolin-CoV (PCoV), human-CoV (hCoV), MERS-CoV (MCoV), Avian-CoV (ACoV) and PEDV1-CoV. Further studies show that subdomains from SARS-CoV 2 RBD Pro³²²-Thr⁵⁸¹, SARS-CoV RBD Pro³⁰⁹-Pro⁵⁷⁵, BtRsRaTG13

SUBMITTER: Pagadala NS 

PROVIDER: S-EPMC8087216 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature