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https://bar.utoronto.ca/thalemine/service/ is incorrectDescription | The coronavirus spike is an envelope glycoprotein which aids viral entry into the host cell. The precursor spike protein can be cleaved into three chains: spike protein S1, S2 and S2'. Spike protein S1 attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. Spike protein S2 mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Spike protein S2' acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis [ , ].S1 contains two major domains: an N-terminal domain (NTD) and a receptor-binding domain (S1 RBD) also referred to as the S1 CTD or domain B. Either the S1 NTD or S1 RBD, or occasionally both, are involved in binding the host receptors [ ].This entry represents an additional, short domain found at the very C terminus of the S1 protein. It is found across a range of alpha, beta and gamma coronaviruses. This small all-β-stranded domain is known as subdomain 2 in the structure of the porcine epidemic diarrhea virus spike protein [ ]. | Name | Coronavirus spike glycoprotein S1, C-terminal |
Short Name | CoV_S1_C | Type | Domain |