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The Journal of Immunology, Vol 155, Issue 4 1921-1929, Copyright © 1995 by American Association of Immunologists

ARTICLES

Differential stability of HLA-DR alleles independent of endogenous peptides

B Devaux, KJ Wilson, B Aguilar, B Jorgensen and JB Rothbard
ImmuLogic Pharmaceutical Corporation, Palo Alto, CA 94305, USA.

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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