Work in my laboratory is centered around an understanding of the relationship between protein structure and function and in particular, how the protein structure relates to catalysis, metal binding, and cooperativity in enzyme systems. For these studies we use a variety of techniques ranging from molecular biology to X-ray crystallography. We are also combining the knowledge gained from these structural and functional studies to develop new classes of inhibitors that can potentially become drugs from the treatment of viral infections, malaria, diabetes and cancer.
Representative Key Publications:
Murphy, J. E., Stec, B., Ma, L., and Kantrowitz, E. R. (1997) Trapping and visualization of a covalent enzyme-phosphate intermediate. Nature Struct. Biol. 4, 618-621.
Macol, C. P., Tsuruta, H., Stec, B., and Kantrowitz, E. R. (2001) Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase. Nat. Struc. Biol. 8, 423-426.
Wang, J., Stieglitz, K. A., Cardia, J. P., and Kantrowitz, E. R. (2005) Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase. Proc. Natl. Acad. Sci. U. S. A. 102, 8881-8886.