Our objectives in this project have been to examine the interaction of self and antigenic peptides with the MHC class I molecule using several different systems and to evaluate these interactions in three dimensional computer modeling studies based on crystallographic MHC structures. Such studies permit us to examine underlying biochemical rules that govern the interaction of antigenic peptides with MHC molecules, a central role in the initiation of the immune response. In addition they provide a framework for understanding the larger question of how proteins bind small molecular weight peptide ligands. Major accomplishments in the past year include the development of quantitative kinetic assays for measurement of the interaction of peptides with purified MHC molecules in real time, and the extensive analysis of the binding of a large number of peptides. Characterization of self peptides has provided the basis for the production of a large number of molecular models of MHC/peptide complexes and permits the more detailed description of the molecular rules that contribute to stable binding.
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