is in the Department of Biochemistry at the University of California, San Francisco where he has served as Chair and Vice Chair. He is also jointly appointed with the Departments of Pharmaceutical Chemistry and Cellular and Molecular Pharmacology at UCSF. Robert is a world-renowned researcher in the area of structural biology. His laboratory has determined high-resolution X-ray crystal structures of nuclear receptors, kinesin molecular motors, clathrin, and many enzymes. He is known for his work on constructing engineered proteins with new function. For about ten years from 1975-1985, the structures of glycogen phosphorylase determined in his lab were record holders. Glycogen phosphorylase, which controls glucose metabolism but knowing when to degrade glycogen to feed the glycolytic pathway, was the largest molecule imaged by X-ray crystallography. Robert Fletterick’s laboratory solved the first structure of a nuclear receptor bound to its hormone and the first structure of the molecular motor kinesin found in nerve cells, showing it related to the well known myosin motor protein of muscle. Presently his lab studies hormone receptors that regulate embryogenesis, steroid metabolism and prostate development and cancer.
Robert received his Ph.D. from Cornell University and did his postdoctoral research in molecular biophysics in the laboratory of Dr. Thomas Steitz at Yale University. Before settling at UCSF, Robert was a professor of Biochemistry at the University of Alberta, and a founding member of the MRC Group on Protein Structure and Function. He has coauthored over two hundred eighty basic science papers.
Dr. Fletterick was elected to the National Academy of Sciences, April 2010.