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Arthritis Rheum. 1995 Dec;38(12):1744-53.

Negatively charged residues interacting with the p4 pocket confer binding specificity to DRB1*0401.

Author information

1
Searle/Monsanto Co., St. Louis, MO 63198, USA.

Abstract

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.

PMID:
8849346
DOI:
10.1002/art.1780381207
[Indexed for MEDLINE]

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