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Conformational changes induced in the MHC class I molecule by peptide and β2-microglobulin

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Abstract

Assembly of the class I MHC molecule is inextricably linked to the antigen presentation function of the class I molecule. Association of the class I MHC molecule with β2-microglobulin (β2m) is a prerequisite for association with the heterodimeric protein TAP, and once peptide is acquired, the class I molecule folds and begins its sojourn to the cell surface. To maintain its folded conformation, class I MHC requires peptide but not β2m, and the sequence of the peptide bound exercises a subtle influence on the structure of the class I molecule that is likely to be a factor in T cell receptor discrimination of MHC/peptide complexes.

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Solheim, J.C., Cook, J.R. & Hansen, T.H. Conformational changes induced in the MHC class I molecule by peptide and β2-microglobulin. Immunol Res 14, 200–217 (1995). https://doi.org/10.1007/BF02918217

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