title: Differential stability of HLA-DR alleles independent of endogenous peptides.
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.
authors.affiliation: ImmuLogic Pharmaceutical Corporation, Palo Alto, CA 94305, USA.
authors.forename: B
authors.initials: B
authors.lastname: Devaux
authors.forename: K J
authors.initials: KJ
authors.lastname: Wilson
authors.forename: B
authors.initials: B
authors.lastname: Aguilar
authors.forename: B
authors.initials: B
authors.lastname: Jorgensen
authors.forename: J B
authors.initials: JB
authors.lastname: Rothbard
mesh_terms: 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
chemical_list: D006684:HLA-DR Antigens; D059811:HLA-DRB1 Chains; C553505:HLA-DRB1*04:01 antigen; D010455:Peptides