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We use a multidisciplinary approach to probe the structure and function of one of the simplest members of the protein kinase family, cAMP-dependent protein kinase (cAPK). PKA serves as a prototype for the entire family of protein kinases. Protein chemistry, kinetics, fluorescence, and X-ray crystallography are among the methods that are employed in our biophysical studies of cAPK structure and function. In parallel, we are studying the dynamic properties of PKA in the cell using recombinant and fluorescence methods. Of particular interest is the role of PKA Anchoring Proteins (AKAPs) which target PKA to specific sites within the cell such as mitochondria.

Track(s):
Molecular Pharmacology


BMS Focus Areas:
Structural Chemical Biology