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The Human TCell Receptor Repertoire and Transplantation (Molecular Biology Intelligence Unit),Used
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these analyses it became clear that the MHC class I molecule com prised a distinct groove on the external side of the molecule. The sides of the groove are formed by the ahelical structures of the a and a 1 2 domains and a floor which is formed by 8 antiparallel 13 strands. The various polymorphic residues, as determined from DNA sequence analysis, are localized within these ahelices and 13plated sheets within the groove. More importantly, these analyses also revealed the presence of elec trondense material in the groove. This material was subsequently iden 568 10 tified as a linear peptide of 810 amino acids long. High resolu tion crystallographic analyses of the class I MHC structure have revealed the existence of socalled pockets within the grooves of the MHC class I molecules. These pockets designated AF, exhibited allelespecificity and are directly involved in the binding of the peptide, primarily through interaction with the dominant anchor residues as found in MHC class I associated pep tides. 6,7,9,11 The class II MHC antigens consist on the cell surface of a 34 kD a chain noncovalently associated with a 28 kD 13 chain. With the excep tion of the DR achain, all other MHC class II a and 13 chains are poly morphic.
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