Article
Differential stability of HLA-DR alleles independent of endogenous peptides.
Journal of immunology (Baltimore, Md. : 1950) - 15 Aug 1995
Devaux B, Wilson K J, Aguilar B, Jorgensen B, Rothbard J B
Abstract excerpt
Purified HLA DRB1*0101 was shown to be inherently more stable to dissociation than DRB1*0401. The residues responsible for the differential stability were defined by constructing hybrid molecules, which contained a small number of residues from DRB1*0101 substituted into the framework of DRB1*0401. One of the hybrid molecules, containing six substituted amino acids, was as stable as DRB1*0101, but exhibited the...
Topics
- Alleles
- Binding Sites
- HLA-DR Antigens
- HLA-DRB1 Chains
- Humans
- Peptides
- Polymorphism, Genetic
- Structure-Activity Relationship