In  the responsive immune system major histocompatibility complex class I (MHC I) proteins plays a key role in the recognition of intracellular pathogens (virus and cancer). The main task of the MHC-I proteins is to present antigens, which may impose a hazard to the cell. The antigen processing and loading onto MHC-I molecules takes place in the intracellular environment, when the antigen-MHC-I complex is transferred to the cell surface for detection by circulating CD8 + T cells. The mechanism of this antigen presentation involves the formation of a so-called MHC-I peptide-loading complex (PLC) where several proteins are involved. One of these proteins, which help to stabilize, facilitate and edit the peptide-loading complex, is Tapasin, a chaperone transmembrane protein.  We are interested in investigating the solution structure and behavior of Tapasin in a first step to understand the connection between that and its biological function. The project is done in collaboration with Kajsa M. Paulsson, head of the Antigen Presentation group at the Faculty of Medicine.

People: Weimin Li, Kajsa M. Paulsson (Experimental Medical Science, Faculty of Medicin), Malin Zackrisson Oskolkova.

Contact person:Malin Zackrisson Oskolkova