Structural and functional significance of the amino acid differences Val₃₅Thr, Ser₄₆Ala, Asn₆₅Ser, and Ala₉₄Ser in 3C-like proteinases from SARS-CoV-2 and SARS-CoV.

ABSTRACT: Three dimensional structures of (chymo)trypsin-like proteinase (3CL^pro) from SARS-CoV-2 and SARS-CoV differ at 8 positions. We previously found that the Val₈₆Leu, Lys₈₈Arg, Phe₁₃₄His, and Asn₁₈₀Lys mutations in these enzymes can change the orientation of the N- and C-terminal domains of 3CL^pro relative to each other, which leads to a change in catalytic activity. This conclusion was derived from the comparison of the structural catalytic core in 169 (chymo)trypsin-like proteinases with the serine/cysteine fold. Val₃₅Thr, Ser₄₆Ala, Asn₆₅Ser, Ala₉₄Ser mutations were not included in that analysis, since they are located far from the catalytic tetrad. In the present work, the structura

SUBMITTER: Denesyuk AI 

PROVIDER: S-EPMC8580570 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature