Selected article for: "CoVs group and table s1"
Author: Chuck, Chi-Pang; Chow, Hak-Fun; Wan, David Chi-Cheong; Wong, Kam-Bo
Title: Profiling of Substrate Specificities of 3C-Like Proteases from Group 1, 2a, 2b, and 3 Coronaviruses
  • Document date: 2011_11_2
    • ID: 0vu7bobr_10
    Snippet: The most preferred P1 residue is Gln (Figure 1 ), which forms hydrogen-bonds with the side-chain of an invariant His residue and the backbone carbonyl group of an invariant Phe residue (His-163 and Phe-140 in SARS-CoV 3CL pro ) in the P1 binding pocket. Interestingly, our results showed that 3CL pro from all groups of CoVs can cleave His at P1 position reasonably well. The relative activities for 3CL pro from HCoV-NL63, HCoV-OC43, SARS-CoV, and I.....
    Document: The most preferred P1 residue is Gln (Figure 1 ), which forms hydrogen-bonds with the side-chain of an invariant His residue and the backbone carbonyl group of an invariant Phe residue (His-163 and Phe-140 in SARS-CoV 3CL pro ) in the P1 binding pocket. Interestingly, our results showed that 3CL pro from all groups of CoVs can cleave His at P1 position reasonably well. The relative activities for 3CL pro from HCoV-NL63, HCoV-OC43, SARS-CoV, and IBV were 0.2660.08, 0.4760.08, 0.1960.03 and 0.2560.12, respectively (Table S1 ). Consistent with this observation, His is found natively at P1 positions in the polyproteins from group 1 and 2a CoVs (Table S3) . Taken together, the ability to cleave His at P1 position is a conserved property for all 3CL pro . Moreover, we showed that all 3CL pro can cleave Q1M, albeit at an even lower rate, and all other substitutions resulted in undetected activity.

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