User:Dora Bonadio/Sandbox 1: Difference between revisions
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== Function == | == Function == | ||
The Mpro protein function is mainly deduced from the function of SARS-CoV virus Mpro , which has a 96% amino acid identity and a highly similar three-dimensional structure with SARS-CoV-2 Mpro <ref> | The Mpro protein function is mainly deduced from the function of SARS-CoV virus Mpro , which has a 96% amino acid identity and a highly similar three-dimensional structure with SARS-CoV-2 Mpro <ref> Zhang L, Lin D, Sun X, Curth U, Drosten C, Sauerhering L, et al. Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors. Science. 2020 Mar 20</ref>(1). As a protease, Mpro is an enzyme that causes proteolysis, which means that it breaks protein peptide bonds by hydrolysis (4). Indeed, the Mpro processes the replicase polyprotein 1ab (pp1ab ~790 kDa) translated from the viral RNA ORF1ab (1, 5). In fact, Mpro cleaves 11 sites of pp1ab and the recognition sequence at most sites is between Leu-Gln and (Ser, Ala, Gly) (1, 3). Proteins resulting from this polyprotein cleavage are non-structural proteins (NSPs) and they seem to contribute with viral replication and transcription (5). Thus, by processing an important number of non-structural proteins, this enzyme plays a critical role in SARS-CoV-2 replication. | ||