Wei-Jen Tang, Ph.D.

Primary:

Professor, Ben May Department for Cancer Research

Secondary:

Committee on Microbiology
Committee on Neurobiology
Committee on Cancer Biology
Committee on Cellular and Molecular Physiology
The College

Education:
Degree Year Institution Area
BS
1982
National Tawian University            
Zoology
PhD
1988
  
University of Texas, Austin
Biological Sciences
Postdoc
1998
University of Texas, Austin
Microbiology
Postdoc
1988-1991
University of Texas Southwestern Medical School
Pharmacology


Phone: (773) 702-4331
E-Mail: wtang@uchicago.edu
Address: Center for Integrative Science, Room W434
Web page:
 http://tang.bsd.uchicago.edu

Research Summary

Molecular and structural basis of cell signal transduction; Protein- and small-molecule-based drug lead discovery for human diseases

The research of my laboratory focuses on elucidating the structural and molecular basis of the interaction of protein with their partner proteins or ligand/drug. Currently, my laboratory has the following projects:
 

Some Selected Papers

Tang, W.-J. and Gilman, A. G.  Type-specific regulation of adenylyl cyclase by G protein betagamma subunits. Science, 254:1500-1503, 1991.

Tang, W.-J., Krupinski, J. and Gilman, A.G.  Expression and characterization of calmodulin activated (type I) adenylyl cyclase. J. Biol. Chem., 266:8595-8603, 1991.

Tang, W.-J. and Gilman, A.G.  Forskolin and Gs-alpha sensitive soluble adenylyl cyclase. Science, 268:1769-1772, 1995.

Yan, S.-Z., Hahn, D., Huang, Z.-H. and Tang, W.-J.  Two cytoplasmic domains of mammalian adenylyl cyclase form a Gsalpha and forskolin-activated enzyme in vitro. J. Biol. Chem., 271:10941-10945, 1996.

Yan, S.-Z., Huang, Z.-H., Rao, V.D., Hurley, J.H. and Tang, W.-J.  Three discrete regions of mammalian adenylyl cyclase form a site for Gs-alpha activation. J. Biol.Chem., 272:18849-18854, 1997.

Yan, S.-Z., Huang, Z.-H., Shaw, R.S. and Tang,W.-J.  The conserved aspargine and arginine are crucial for catalysis of mammalian adenylylcyclase. J. Biol. Chem., 272:12342-12349, 1997.

Yan,S.-Z., Huang, Z.-H., Andrews R.K. and Tang,W.-J.  Conversion of forskolin insensitive to sensitive (mouse type IX) adenylyl cyclase. Mol. Pharm., 53:182-187, 1998.

Drum, C.L., Yan, S.-Z., Sarac, R., Mabuchi, Y., Beckingham, K., Bohm, A., Grabarek, Z. and Tang, W.-J. An extended conformation of calmodulin induces interactions between the structural domains of adenylyl cyclase from Bacillus anthracis to promote catalysis. J. Biol. Chem., 275:36334-36340, 2000.

Yan, S.-Z. Beeler, J. Chen, Y., Shelton, R.K. and Tang, W.-J.  The regulation of human type 7 adenylyl cyclase by C1b and E. coli peptidyl prolyl isomerase, SlyD.  J. Biol. Chem., 276: 8500-8506, 2001.

Drum, C.L., Yan, S.-Z.,  Bard, J., Shen, Y.-Q., Lu, D., Soelaiman, S., Grabarek, Z., Bohm, A. and Tang, W.-J.  Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. Nature, 415:396-402, 2002.

Shen, Y.-Q., Lee, Y.-S., Soelaiman, S., Bergson, P., Lu, D., Chen, A., Beckingham, K., Grabarek, Z., Mrksich, M. and Tang, W.-J. Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins. EMBO J., 21: 6721-6732, 2002.

Soelaiman, S., Wei, B., Bergson, P., Lee, Y.-S., Shen, Y., Mrksich, M., Shoichet, B. and Tang, W.-J.  Structure-based inhibitor discovery against anthrax adenylyl cyclase toxins from pathogenic bacteria that cause anthrax and whooping cough. J. Biol. Chem., 278:25990-25997, 2003.

Shen, Y.-Q., Zhukovskaya, N.L., Zimmer, M.I., Soelaiman, S., Wang, C.R., Gibbs, C.S. and Tang, W.-J.  Selective inhibition of anthrax edema factor by adefovir, a drug for chronic hepatitis B virus infection. Proc. Natl. Acad. Sci. U.S.A., 101:3242-3247, 2004.

Guo, Q., Shen, Y.-Q., Zhukovskaya, N.L., Florian, J. and Tang, W.-J.  Structural and kinetic analyses of the interaction of anthrax adenylyl cyclase toxin with reaction products, cAMP and pyrophosphate. J. Biol. Chem., 279:29427-29435, 2004.

Lee, Y.-S., Bergson, P., He, W.-S., Mrksich, M. and Tang, W.-J. Discovery of a small molecule that inhibits the interaction of anthrax edema factor with its cellular activator, calmodulin. Chem. and Biol., 11:1139-1146, 2004.

Beeler, J.A., Yan, S.-Z., Bykov, S., Murza, A., Asher, S. and Tang, W.-J.  A stable C1b soluble protein and its regulation of soluble type 7 adenylyl cyclase: a prototype for soluble C1b model. Biochemistry, 43(49):15463-15471, 2004.

Shen, Y., Zhukovskaya, N.L., Guo, Q., Florian, J. and Tang, W.-J. Calcium-independent calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor. EMBO J., 24:929-941, 2005.

Guo, Q., Shen, Y., Lee, Y.-S., Gibbs, C.S., Mrksich, M. and Tang, W.-J. Structural basis for the interaction of adenylyl cyclase toxin of Bordetella pertussis with calmodulin. EMBO J., 24:3190-3201, 2005.

Shen, Y., Joachimiak, A., Rosner, M.R. and Tang, W.-J. Structures of human insulin degrading enzyme reveal a new substrate recognition mechanism. Nature, 443:870-874, 2006.

Im, H., Manolopoulou, M., Malito, E., Shen, Y., Zhao, J., Neant-Fery, M., Sun, C.Y., Meredith, S.C., Sisodia, S.S., Leissring, M..A. and Tang W.J. Structure of Substrate-free Human Insulin-degrading Enzyme (IDE) and Biophysical Analysis of ATP-induced Conformational Switch of IDE. J. Biol. Chem., 282(35):25453-63, 2007.

Updated 9/24/07.