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Binding of truncated peptides to the MHC molecule IA d
Author(s) -
Dornmair Klaus,
Clark Brian R.,
McConnell Harden M.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81439-f
Subject(s) - peptide , histidine , chemistry , amino acid , ovalbumin , stereochemistry , peptide sequence , molecule , biochemistry , biology , antigen , genetics , organic chemistry , gene
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 α‐ and β‐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.