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I major histocompatibility complex (MHC) molecules are ternary complexes of the soluble serum protein beta 2-microglobulin, MHC heavy chain, and bound peptide. The first two domains (alpha 1, alpha 2) of the heavy chain create the peptide binding cleft and the surface that contacts the T-cell receptor. The third domain (alpha 3) associates with the T-cell co-receptor, CD8, during T-cell recognition. Here we describe the x-ray crystal structure of a human class I MHC molecule, HLA-Aw68, from which the alpha 3 domain has been proteolytically removed. The resulting molecule shows no gross morphological changes compared to the intact protein. A decameric peptide complexed with the intact HLA-Aw68 is seen to bind to the proteolized molecule in the conventional manner, demonstrating that the alpha 3 domain is not required for the structural integrity of the molecule or for peptide binding.","bibjson":{"author":[{"initials":"EJ","lastname":"Collins","name":"Collins EJ"},{"initials":"DN","lastname":"Garboczi","name":"Garboczi DN"},{"initials":"MN","lastname":"Karpusas","name":"Karpusas MN"},{"initials":"DC","lastname":"Wiley","name":"Wiley DC"}],"identifier":[{"id":"10.1073/pnas.92.4.1218","type":"doi"},{"id":"7862664","type":"pubmed"}],"issue":["4"],"journal":{"iso_abbreviation":"Proc. Natl. Acad. Sci. 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