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Binding of truncated peptides to the MHC molecule IA (d)
K Dornmair1, B R Clark, H M McConnell
1Stauffer Laboratory for Physical Chemistry, Stanford University, CA 94305.
FEBS Letters
|December 9, 1991
Abstract:
A peptide comprising amino acids 323-339 of chicken ovalbumin is known to bind to two heterodimeric conformations of the MHC molecule IA(d), and to each of its separate alpha- and beta-chains. We report that minor C- and N-terminal truncations of the parent peptide do not alter the binding pattern. A decrease in binding activity was observed upon deletion of the histidine residues of the already truncated peptides. Peptides as short as 4 amino acids associate weakly with all four proteins.