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Structural basis of mercury- and zinc-conjugated complexes as SARS-CoV 3C-like protease inhibitors
Authors:Lee Cheng-Chung  Kuo Chih-Jung  Hsu Min-Feng  Liang Po-Huang  Fang Jim-Min  Shie Jiun-Jie  Wang Andrew H-J
Institution:Structural Biology Program, Institute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei 11221, Taiwan.
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.
Keywords:BABIM  bis(5-amidino-2-benzimidazolyl) methane  EPDTC  N-ethyl-N-phenyldithiocarbamic acid zinc  ESI-MS  electrospray ionization mass spectrometry  JMF1586  l-aspartato-N" target="_blank">bis(l-aspartato-N  O) zinc(II) ethanate  JMF1600  (nitrilotriacetato-N  O) zinc(II) acetate  NMR  nuclear magnetic resonance  PMA  phenylmercuric acetate  TDT  toluene-3  4-dithiolato zinc
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