Related Experiment Video
Updated: Aug 1, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
Negatively charged residues interacting with the p4 pocket confer binding specificity to DRB1*0401
S L Woulfe1, C P Bono, M L Zacheis
1Searle/Monsanto Co., St. Louis, MO 63198, USA.
Objective:
To identify critical residues involved in the binding of a selective peptide to DRB1*0401.
Methods:
The binding of peptides to native or site-directed mutant DR molecules was evaluated using enzyme-linked immunosorbent assay and flow cytometry.
Results:
Amino acid substitutions at DR and peptide residues, which were predicted to contribute to interactions within the DR p4 pocket, had the greatest effects on the specificity of binding.
Conclusion:
Differences in the peptide-binding repertoires of DR molecules may contribute to associations with autoimmune diseases.
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