Abstract:

In this study, 27 protein sequences of SARS-CoV-2 spike (S) glycoprotein from 23 different countries were analyzed using bioinformatics approaches. In this context, post-translational modifications, sequence and domain analyses, phylogenetic analysis, and 3D structure analysis of the spike glycoprotein proteins were performed. Also, molecular docking analysis of the SARS-CoV-2 spike protein S1 receptor-binding domain (SS1) with human ACE2 protein was conducted. It was found that although all SARS-CoV-2s include Spike_rec_bind (PF09408) and Corona_S2 (PF01601) domain structures, the C-terminal S2 region was more diverse than the S1 region. The predicted N-glycosylation and phosphorylation sites were determined to be between 17 and 19 and 136 and 168, respectively. In phylogenetic analysis, SARS-CoV-2s were found to have more similarity with bat RaTG13 and pangolin CoV-2 than MERS CoV and bat SARS CoV. The predicted 3D protein structures of human SARS-CoV-2 and bat RaTG13 showed high similarity, ranging from 0.76 to 0.78. The docking analyses revealed that Asp30, Lys31, His34, Glu35, Glu37, Asp38, Asn330, and Gln325 residues were binding residues in the ACE2 protein for the N-terminal S1 subunit of SARS-CoV-2. The findings are particularly important for the studies of drug development and drug design.

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