Molecular Interactions Of Lymphoid Cell Receptors

National Institute Of Allergy And Infectious Diseases

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Abstract

This project takes advantage of the laboratory's expertise in studying molecular interactions and molecular structure. Specifically, following up on our previous structural studies of the tapasin-like molecule, TAPBPR, we have recently determined the X-ray crystallographic structure of the major chaperone component of the peptide-loading complex (PLC), tapasin, in complex with an MHC-I molecule, HLA-B*44:05. This structure extends our knowledge of the structural details of how MHC-I molecules load with peptides, the molecular conformational adjustments that are made by the chaperone, tapasin, to stabilize a peptide receptive conformation of the MHC-I molecule, and the catalytic role that tapasin plays in allowing peptide exchange favoring high affinity peptides. These fundamental observations refine our molecular understanding the peptide loading process. In addition to these structural studies, we have generated TAPBPR knockout mice and are studying the role of TAPBPR and tapasin in the processes of antigen presentation and cross-presentation.