@article{247ff4ba2e064a7ab5aab3525bbc718c,
title = "Structural basis of mercury- and zinc-conjugated complexes as SARS-CoV 3C-like protease inhibitors",
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: Hg2+-PMA is coordinated to C44, M49 and Y54 with a square planar geometry at the S3 pocket, whereas each Zn2+ of the four zinc-inhibitors is tetrahedrally coordinated to the H41-C145 catalytic dyad. For anti-SARS drug design, this Zn2+-centered coordination pattern would serve as a starting platform for inhibitor optimization.",
keywords = "Metal ion, Protease inhibitor, SARS",
author = "Lee, {Cheng Chung} and Kuo, {Chih Jung} and Hsu, {Min Feng} and Liang, {Po Huang} and Fang, {Jim Min} and Shie, {Jiun Jie} and Wang, {Andrew H.J.}",
note = "Funding Information: We acknowledge the National Synchrotron Radiation Research Center of Taiwan, SPring-8 of Japan for beam time allocation. We thank Dr. T.-P. Ko for critical review of the manuscript. This work was supported by grants from Academia Sinica and the National Science Council, Taiwan NSC-93-3112-B-001-011-Y to A.H.-J. Wang for the National Core Facility of High-Throughput Protein Crystallography at Academia Sinica, Taiwan. ",
year = "2007",
month = nov,
day = "27",
doi = "10.1016/j.febslet.2007.10.048",
language = "English",
volume = "581",
pages = "5454--5458",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "John Wiley and Sons Inc.",
number = "28",
}