Abstract
Class II and class I histocompatibility molecules allow T cells to recognize 'processed' polypeptide antigens1–5. The two polypeptide chains of class II molecules, α and β, are each composed of two domains (for review see ref. 6); the N-terminal domains of each, α1 and β1, are highly polymorphic6–10 and appear responsible for binding peptides at what appears to be a single site11–13 and for being recognized by MHC-restricted antigen-specific T cells14,15. Recently, the three-dimensional structure of the foreign antigen binding site of a class I histocompatibility antigen has been described16,17. Because a crystal structure of a class II molecule is not available, we have sought evidence in class II molecules for the structural features observed in the class I binding site by comparing the patterns of conserved and polymorphic residues of twenty-six class I and fifty-four class II amino acid sequences. The hypothetical class II foreign-antigen binding site we present is consistent with mutation experiments18–28 and provides a structural framework for proposing peptide binding models to help understand recent peptide binding data11,29–33.
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Brown, J., Jardetzky, T., Saper, M. et al. A hypothetical model of the foreign antigen binding site of Class II histocompatibility molecules. Nature 332, 845–850 (1988). https://doi.org/10.1038/332845a0
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DOI: https://doi.org/10.1038/332845a0
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