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Associate Professor of Microbiology
Office Location(s): 6748 Med. Sci. II
The binding of complexes of peptides and major histocompatibility complex (MHC) class I molecules to T cell receptors is of fundamental importance for the recognition of virally infected cells by T cells. Our major interest is in the MHC class I antigen processing pathway, the cellular pathway by which complexes of peptides and MHC class I molecules are generated. We study specific components of this pathway, including the transporter associated with antigen processing (TAP), tapasin, and calreticulin. TAP transports peptides from the cytosol to the endoplasmic reticulum (ER) for binding to class I MHC molecules, and tapasin is an ER-resident protein that enhances peptide binding by MHC class I molecules. Calreticulin is a generic cellular chaperone in the ER.
Our goal is to understand the mechanism of function of these proteins at the biochemical and structural level. We use molecular biology and biochemical techniques to generate desired proteins in heterologous systems. We investigate mechanisms of function using biochemical and biophysical techniques.
Chemistry BuildingRoom 4028930 N. University Ave.
Ann Arbor, MI