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{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7784829","sourcedb":"PMC","sourceid":"7784829","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7784829","text":"SARS-CoV-2 has a genome of ∼30 kilobases, which codes for multiple structural and non-structural proteins (Chan et al., 2020). The structural proteins, present on the surface of the mature virion, include the spike protein, the membrane protein, the envelope protein and the nucleocapsid protein (Chan et al., 2020). The Spike protein, of the beta coronaviruses SARS-CoV-2 and SARS-CoV, enables the attachment of the virus to the cells of the lower respiratory tract of humans to gain entry into the lung tissue (Hoffmann et al., 2020). Apart from attachment, the spike glycoprotein also appears to play a role in fusion and entry of the virus into the host (Chen et al., 2020; Hoffmann et al., 2020). The spike protein, of the novel coronavirus, utilizes the SARS-CoV receptor, ACE2 for entry (Chen et al., 2020) and is primed by the cellular protease, TMPRSS2 (Hoffmann et al., 2020). A serine protease inhibitor, which can act on TMPRSS2, has been shown to inhibit novel coronavirus entry (Hoffmann et al., 2020). Therefore, the spike protein of the novel coronavirus is a good drug target and identifying small molecules that bind to S protein would inhibit viral recognition of host cells and disrupt viral-host 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