Differential stability of HLA-DR alleles independent of endogenous peptides

J Immunol. 1995 Aug 15;155(4):1921-9.

Abstract

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 binding specificity of DRB1*0401. This result indicated that the differential stability between the alleles arose from structural differences, and was not due solely to varying populations of endogenous peptides.

MeSH terms

  • Alleles*
  • Binding Sites
  • HLA-DR Antigens / chemistry
  • HLA-DR Antigens / genetics*
  • HLA-DR Antigens / metabolism
  • HLA-DRB1 Chains
  • Humans
  • Peptides / metabolism*
  • Polymorphism, Genetic
  • Structure-Activity Relationship

Substances

  • HLA-DR Antigens
  • HLA-DRB1 Chains
  • HLA-DRB1*04:01 antigen
  • Peptides