Protein supercomplexes play central roles in many cellular processes, yet often little is known about their higher-order structural organization. We aim at characterizing the molecular architecture and interactions of the major histocompatibility complex (MHC) class I peptide-loading complex (PLC). This protein complex is a key player in the adaptive immune system.
TMD0 structures predicted from de novo modelling.
We aim at elucidating the structures of the N-terminal TMD0 domains of the heterodimeric ABC transporter TAP1/2. These 4-TM bundles are key interaction hubs in the PLC, and hence we study their interactions with the coreTAP ABC transporter and the chaperone tapasin. Furthermore, we investigate how the other components of the supercomplex arrange themselves around this platform. The ultimate aim is to obtain a detailed picture of the atomistic structure, interactions, and dynamics of the entire PLC. This project is embedded in the collaborative research center Transport and communication across biological membranes (SFB 807).