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Peptides Presented to the Immune System by the Murine Class II Major Histocompatibility Complex Molecule I-A d

1992; American Association for the Advancement of Science; Volume: 256; Issue: 5065 Linguagem: Inglês

10.1126/science.1319610

1095-9203

Donald F. Hunt, Hanspeter Michel, Tracey Dickinson, Jeffrey Shabanowitz, Andrea L. Cox, Kazuyasu Sakaguchi, Ettore Appella, Howard M. Grey, Alessandro Sette,

Immune Cell Function and Interaction

Between 650 and 2000 different peptides are associated with the major histocompatibility complex class II molecule I-Ad. Sequences for nine of these were obtained by a combination of automated Edman degradation and tandem mass spectrometry. All of the peptides are derived from secretory or integral membrane proteins that are synthesized by the antigen-presenting cell itself. Peptides were 16 to 18 residues long, had ragged NH2-and COOH-termini, and contained a six-residue binding motif that was variably placed within the peptide chain. Binding data on truncated peptides suggest that the peptide binding groove on class II molecules can be open at both ends.