Article
Prominent roles of secondary anchor residues in peptide binding to HLA-A24 human class I molecules.
Journal of immunology (Baltimore, Md. : 1950) - 1 Nov 1995
Kondo A, Sidney J, Southwood S, del Guercio M F, Appella E, Sakamoto H, Celis E, Grey H M, Chesnut R W, Kubo R T, Sette A
Abstract excerpt
The binding capacity of large sets of peptides corresponding to naturally occurring sequences and carrying previously defined A24-specific motifs was analyzed. It was found that only a minority (9-25%) of the motif-carrying peptides bound the relevant HLA-A molecule with good affinity (IC 50% < or = 50 nM), while the majority of them bound only weakly or not at all (IC 50% > or = 500 nM). By correlating the...
Topics
- Alleles
- Amino Acid Sequence
- Binding Sites
- Cell Line, Transformed
- HLA-A Antigens
- HLA-A24 Antigen
- Humans
- Molecular Sequence Data
- Peptide Fragments
- Protein Binding