Article
Role of the polymorphic residues in HLA-DR molecules in allele-specific binding of peptide ligands.
Journal of immunology (Baltimore, Md. : 1950) - 15 May 1994
Marshall K W, Liu A F, Canales J, Perahia B, Jorgensen B, Gantzos R D, Aguilar B, Devaux B, Rothbard J B
Abstract excerpt
Analysis of peptide binding to a set of HLA-DR alleles has allowed the proteins to be segregated into functional subsets, depending on the amino acids at positions 57 and 86 of the beta-chain. DR proteins with glycine at 86 beta and aspartic acid at 57 beta bound a simplified peptide with significantly lower IC50 values than alleles that did not have this combination of amino acids. The size of the amino acid at...
Topics
- Alleles
- Amino Acid Sequence
- Binding Sites
- HLA-DR Antigens
- Humans
- Ligands
- Molecular Sequence Data
- Peptide Fragments
- Peptides
- Structure-Activity Relationship