Binding of truncated peptides to the MHC molecule IA (d).
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.
Dornmair
K
K
Stauffer Laboratory for Physical Chemistry, Stanford University, CA 94305.
Clark
B R
BR
McConnell
H M
HM
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002645:Chickens; D000949:Histocompatibility Antigens Class II / Q000378:metabolism*; D046911:Macromolecular Substances; D051379:Mice; D008969:Molecular Sequence Data; D010047:Ovalbumin / Q000737:chemistry / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation
D000949:Histocompatibility Antigens Class II; D046911:Macromolecular Substances; D010455:Peptides; D010047:Ovalbumin