Journal
FEBS LETTERS
Volume 581, Issue 28, Pages 5454-5458Publisher
WILEY
DOI: 10.1016/j.febslet.2007.10.048
Keywords
SARS; metal ion; protease inhibitor
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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: Hg2+-PMA is coordinated to C-44, M-49 and Y-54 with a square planar geometry at the S3 pocket, whereas each Zn2+ of the four zinc-inhibitors is tetrahedrally coordinated to the H-41-C-145 catalytic dyad. For anti-SARS drug design, this Zn2+-centered coordination pattern would serve as a starting platform for inhibitor optimization. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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