Author: Robin Franklin; Adam Young; Bjoern Neumann; Rocio Fernandez; Alexis Joannides; Amir Reyahi; Yorgo Modis
Title: Homologous protein domains in SARS-CoV-2 and measles, mumps and rubella viruses: preliminary evidence that MMR vaccine might provide protection against COVID-19 Document date: 2020_4_10
ID: nd5r4yt4_15
Snippet: The homologous sequences in SARS-CoV-2 and rubella, aligned in PSI-BLAST [Altschul et al., 1997] with an expected value of 10 -78 , encode Macro domains in SARS-CoV-2 non-structural protein 3 (NSP3), a papain-like protease, and in rubella virus p150, a protease/methyltransferase. Macro domains can bind ADP-ribose-1''-phosphate, an NAD metabolite, and have ADP-ribose-1''-phosphatase (ADRP) activity. The presence of Macro domains with ADRP activity.....
Document: The homologous sequences in SARS-CoV-2 and rubella, aligned in PSI-BLAST [Altschul et al., 1997] with an expected value of 10 -78 , encode Macro domains in SARS-CoV-2 non-structural protein 3 (NSP3), a papain-like protease, and in rubella virus p150, a protease/methyltransferase. Macro domains can bind ADP-ribose-1''-phosphate, an NAD metabolite, and have ADP-ribose-1''-phosphatase (ADRP) activity. The presence of Macro domains with ADRP activity in coronaviruses, paramyxoviruses and alphaviruses has been noted previously [Snijder et al., 2003; Saikatendu et al., 2005; Eriksson et al., 2008] . A crystal structure of the SARS-CoV-2 Macro domain bound to ADP-ribose (Protein Data Bank entry 6W02) allows the substrate binding pocket and catalytic residues to be identified, by analogy with other Macro domains.
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