Author: David N. Frick; Rajdeep S. Virdi; Nemanja Vuksanovic; Narayan Dahal; Nicholas R Silvaggi
Title: Variable Macro X Domain of SARS-CoV-2 Retains the Ability to Bind ADP-ribose Document date: 2020_4_2
ID: 02q9y011_4
Snippet: Hypervariability in the nsp3 Macro X domain-The structures of most of the soluble portions of the SARS-CoV-1 nsp proteins have been examined at atomic resolution to help understand coronavirus replication and facilitate antiviral drug discovery. The amino acid sequences of each of these proteins were compared with the homologous regions of the rep 1ab protein encoded by SARS-CoV-2 (GenPept Accession YP_009724389). The most similar proteins were t.....
Document: Hypervariability in the nsp3 Macro X domain-The structures of most of the soluble portions of the SARS-CoV-1 nsp proteins have been examined at atomic resolution to help understand coronavirus replication and facilitate antiviral drug discovery. The amino acid sequences of each of these proteins were compared with the homologous regions of the rep 1ab protein encoded by SARS-CoV-2 (GenPept Accession YP_009724389). The most similar proteins were the RNA helicases (nsp13) which are identical in all but one of their 603 amino acids: a conservative Val to Ile substitution near their C-termini. The RNA-dependent RNA polymerases (nsp12) are also well-conserved, sharing all but 34 of 955 amino acids. The primary protease that cleaves the polyprotein (nsp5) is also similar in SARS-CoV-1 and SARS-CoV-2, with only 13 amino acids that differ among 306 (4.2% different) (Fig. 1 ).
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