NEGATIVELY CHARGED RESIDUES INTERACTING WITH THE P4 POCKET CONFER BINDING-SPECIFICITY TO DRB1-ASTERISK-0401

Objective. To identify critical residues involved in the binding of a selective peptide to DRB10401. Methods. The binding of peptides to na tive or site-directed mutant DR molecules was evaluated using enzyme-l inked immunosorbent assay and flow cytometry. Results. Amino acid subs titutions at DR and peptide residues, which were predicted to contribu te to interactions within the DR p4 pocket, had the greatest effects o n the specificity of binding. Conclusion. Differences in the peptide-b inding repertoires of DR molecules may contribute to associations with autoimmune diseases.