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Science 26 June 1992:
Vol. 256. no. 5065, pp. 1817 - 1820
DOI: 10.1126/science.1319610
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Articles

Science, Vol 256, Issue 5065, 1817-1820
Copyright © 1992 by American Association for the Advancement of Science

articles

Peptides presented to the immune system by the murine class II major histocompatibility complex molecule I-Ad

DF Hunt, H Michel, TA Dickinson, J Shabanowitz, AL Cox, K Sakaguchi, E Appella, HM Grey, and A Sette

Department of Chemistry, University of Virginia, Charlottesville 22901.

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.


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