Proceedings of the National Academy of Sciences of the United States of America

About the PNAS Member Editor
Name Bjorkman, Pamela J.
Location California Institute of Technology
Primary Field Biochemistry
Secondary Field Biophysics and Computational Biology
 Election Citation
Bjorkman pioneered the use of x-ray crystallography to pinpoint the structures of key major histocompatability complex proteins that enable the immune system to discern foreign invaders from harmless self-proteins. After identifying the first crystal structure of a major histocompatability complex protein in 1987, Bjorkman remains a leader in functional and structural studies of other proteins involved in immune responses.
 Research Interests
My laboratory is interested in the structure and function of molecules involved in cell surface recognition, particularly those mediating recognition in the immune system, with special attention to the homologs of class I MHC proteins, which function in many ways that are distinct from their immunological role in peptide presentation to T cells. These include an immunoglobulin G receptor (FcRn), the protein mutated in the iron storage disease hereditary hemochromatosis (HFE), a protein that stimulates lipid catabolism (Zn-alpha-2-glycoprotein; ZAG), and virally encoded class I MHC homologs. To study these proteins we use a combined approach of X-ray crystallography to determine structures, molecular biology to produce proteins for crystallization and to modify them, and biochemistry to study protein-protein interactions. In the FcRn and HFE systems we use structural information to address cell biological issues involving intracellular receptor-ligand trafficking, which we are studying by confocal and electron microscopy. We are also interested in bacterial pathogenesis and the innate immune response to bacterial infection. Our efforts in these areas involve the study of the Yersinia pseudotuberculosis protein invasin, the insect immune response protein hemolin, the mammalian mannose receptor, and inhibitory receptor-ligand interactions.

 
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