Differential stability of HLA-DR alleles independent of endogenous peptides.
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.
Devaux
B
B
ImmuLogic Pharmaceutical Corporation, Palo Alto, CA 94305, USA.
Wilson
K J
KJ
Aguilar
B
B
Jorgensen
B
B
Rothbard
J B
JB
D000483:Alleles; D001665:Binding Sites; D006684:HLA-DR Antigens / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D059811:HLA-DRB1 Chains; D006801:Humans; D010455:Peptides / Q000378:metabolism*; D011110:Polymorphism, Genetic; D013329:Structure-Activity Relationship
D006684:HLA-DR Antigens; D059811:HLA-DRB1 Chains; C553505:HLA-DRB1*04:01 antigen; D010455:Peptides