PMC:7216760 / 10288-11855 JSONTXT

{"target":"http://pubannotation.org/docs/sourcedb/PMC/sourceid/7216760","sourcedb":"PMC","sourceid":"7216760","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7216760","text":"Potential Drug Targets\nSARS-CoV-2 viral RNA encodes several proteins that are potentially druggable targets (Figure 1 and Table S2), including four structural proteins: the Spike (S), Envelope (E), Membrane (M), and Nucleocapsid (N).1 The 1273 amino acid, 141 kDa, Spike protein is heavily N-glycosylated and is a major inducer of host immune responses. The 222 amino acid M protein has three transmembrane domains and is the most abundant structural protein in the virion. The 75 amino acid E protein is important for assembly and release of the virus. The 419 amino acid nucleocapsid protein forms a protective protein shell around the virus genetic material and is encased in a lipid envelope that is usurped from the host cell. Matrix protein connects the membrane to the nucleocapsid protein. There are also 16 nonstructural proteins (nsp1–16)1 including several for which there are X-ray crystallography-derived structural data: RNA dependent RNA polymerase (nsp12, RdRp), a papain-like protease (nsp3, PLpro), the main protease (nsp5, 3CLpro, or Mpro), and exonuclease/N7-methyltransferase (nsp14, ExoN). RdRp catalyzes synthesis of the full length negative-strand RNA template used by RdRp to make more viral genomic RNA. The SARS-CoV-2 genome also contains a number of open reading frames (ORFs): namely, ORF 1a proposed to encode nsp1 to nsp11; ORF1b, is proposed to encode nsp12 to nsp16, essential for viral replication, and ORFs 3a, 3b, 6, 7a, 7b, 8, 9a, 9b, and 10, which encode for accessory proteins1 (Table S2).\nFigure 1 SARS-CoV-2 encoded 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