Selected article for: "adp ribose and amino acid"

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_5
    Snippet: At the other end of the spectrum are the nsp3 proteins, which are notably more different in the two SARS viruses. Nsp3 is a large multidomain membrane-bound protein, 6 and its clearest role in viral replication is cleaving the rep polyprotein. Over 17% of the amino acids in the nsp3 protease domain differ between SARS-CoV-1 and SARS-CoV-2. Other parts of nsp3 are even more variable, like the macrodomains that lie N-terminal to the nsp3 protease d.....
    Document: At the other end of the spectrum are the nsp3 proteins, which are notably more different in the two SARS viruses. Nsp3 is a large multidomain membrane-bound protein, 6 and its clearest role in viral replication is cleaving the rep polyprotein. Over 17% of the amino acids in the nsp3 protease domain differ between SARS-CoV-1 and SARS-CoV-2. Other parts of nsp3 are even more variable, like the macrodomains that lie N-terminal to the nsp3 protease domain. Macrodomains consist of four helices that surround a mixed beta sheet. A ligand-binding pocket that typically binds ADP-ribose or related compounds lies between the helices and the sheet. 7 SARS-CoV-1 has three macrodomains in tandem, but only the first binds ADP ribose. The amino acid sequences of this macro X domain differ by 26% between SARS-CoV-1 and SARS-CoV-2 ( Fig. 1) .

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