Research Abstract:
The laboratory is interested in the molecular basis of protease specificity and allosteric regulation. Our studies involve a combination of kinetics, thermodynamics, site-directed mutagenesis and X-ray structural methods. Current efforts are focused on the redesign of protease specificity toward substrates and monovalent cations and the structure of protein complexes of physiological relevance.
Selected Publications:
Di Cera E. Engineering protease specificity made simple, but not simpler. Nat Chem Biol 2008 4:270-271.
Page MJ, Di Cera E. Serine peptidases: classification, structure and function. Cell Mol Life Sci 2008 65:1220-1236.
Di Cera E. Thrombin. Mol Aspects Med 2008 29:203-254.
Gandhi PS, Chen Z, Mathews FS, et al. Structural identification of the pathway of long-range communication in an allosteric enzyme. Proc Natl Acad Sci USA 2008 105:1832-1837.
Bah A, Chen Z, Bush-Pelc LA, et al. Crystal structures of murine thrombin in complex with the extracellular fragments of protease-activated receptors PAR3 and PAR4. Proc Natl Acad Sci USA 2007 104:11603-11608.
Last Updated: 07/31/2008 |