Binding of truncated peptides to the MHC molecule IA (d). |
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| Authors: | K Dornmair B R Clark H M McConnell |
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| Affiliation: | Stauffer Laboratory for Physical Chemistry, Stanford University, CA 94305. |
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| 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. |
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