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Homology models of main proteinase from coronavirus associated with SARS.

ABSTRACT: In this study, two homology models of the main proteinase (M^pro) from the novel coronavirus associated with severe acute respiratory syndrome (SARS-CoV) were constructed. These models reveal three distinct functional domains, in which an intervening loop connecting domains II and III as well as a catalytic cleft containing the substrate binding subsites S1 and S2 between domains I and II are observed. S2 exhibits structural variations more significantly than S1 during the 200 ps molecular dynamics simulations because it is located at the open mouth of the catalytic cleft and the amino acid residues lining up this subsite are least conserved. In addition, the higher structural variation of S2 makes it flexible enough to accommodate a bulky hydrophobic residue from the substrate.

SUBMITTER: Liu HL

PROVIDER: S-EPMC7094242 | biostudies-literature | 2005 Jan

REPOSITORIES: biostudies-literature

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Homology models of main proteinase from coronavirus associated with SARS.

Liu Hsuan-Liang HL Lin Jin-Chung JC Ho Yih Y Chen Chin-Wen CW

Chemical physics letters 20041123 1

In this study, two homology models of the main proteinase (M<sup>pro</sup>) from the novel coronavirus associated with severe acute respiratory syndrome (SARS-CoV) were constructed. These models reveal three distinct functional domains, in which an intervening loop connecting domains II and III as well as a catalytic cleft containing the substrate binding subsites S1 and S2 between domains I and II are observed. S2 exhibits structural variations more significantly than S1 during the 200 ps molec ...[more]

PMID: 32226085

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