Abstract
Five active metal-conjugated inhibitors (PMA, TDT, EPDTC, JMF1586 and JMF1600) bound with the 3C-like protease of severe acute respiratory syndrome (SARS)-associated coronavirus were analyzed crystallographically. The complex structures reveal two major inhibition modes: Hg 2+-PMA is coordinated to C 44, M 49 and Y 54 with a square planar geometry at the S3 pocket, whereas each Zn 2+ of the four zinc-inhibitors is tetrahedrally coordinated to the H 41–C 145 catalytic dyad. For anti-SARS drug design, this Zn 2+-centered coordination pattern would serve as a starting platform for inhibitor optimization.
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