Differential stability of HLA-DR alleles independent of endogenous peptides.

B Devaux, KJ Wilson, B Aguilar… - … (Baltimore, Md.: 1950 …, 1995 - journals.aai.org
B Devaux, KJ Wilson, B Aguilar, B Jorgensen, JB Rothbard
Journal of immunology (Baltimore, Md.: 1950), 1995journals.aai.org
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 …
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.
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