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Figure 1.
Fig. 1. The SARS-CoV Mpro dimer structure complexed with a
substrate-analogue hexapeptidyl CMK inhibitor. (A) The SARS-CoV
Mpro dimer structure is presented as ribbons, and inhibitor
molecules are shown as ball-and-stick models. Protomer A (the
catalytically competent enzyme) is red, protomer B (the inactive
enzyme) is blue, and the inhibitor molecules are yellow. The
N-finger residues of protomer B are green. The molecular surface
of the dimer is superimposed. (B) A cartoon diagram illustrating
the important role of the N-finger in both dimerization and
maintenance of the active form of the enzyme.
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