Amino acid sequence of the carboxyl-terminal hydrophilic region of the H-2Kb MHC alloantigen. Completion of the entire primary structure of the H-2Kb molecule.

The amino acid sequence of the COOH-terminal hydrophilic region of the H-2Kb histocompatibility antigen was determined. The sequence was completed by analyses of four CNBr fragments obtained from the intact molecule as well as tryptic peptides. This region was composed of 39 amino acid residues with a cluster of basic residues at the NH2 terminus and localized positions 308-346 of the H-2Kb molecule. These sequence data, together with those reported for the NH2-terminal 284 residues [Martinko, J. M., Uehara, H., Ewenstein, B. M., Kindt, T. J., Coligan, J. E., & Nathenson, S. G. (1980) Biochemistry 19, 6188-6193] and for the intramembranous segment [Uehara, H., Coligan, J. E., & Nathenson, S. G. (1981) Biochemistry (preceding paper in this issue)], provided the complete primary structure of the H-2Kb molecule. This is the first histocompatibility antigen for which the entire primary structure is determined.