Negatively charged residues interacting with the p4 pocket confer binding specificity to DRB1*0401
| Autor: | Robert W. Karr, Christine P. Bono, D.A. Kirschmann, Michelle L. Zacheis, Benjamin D. Schwartz, Troy A. Baudino, Craig Swearingen, Susan L. Woulfe |
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| Rok vydání: | 1995 |
| Předmět: |
Molecular Sequence Data
Immunology Mutant Enzyme-Linked Immunosorbent Assay Peptide Biology Protein Structure Secondary Flow cytometry Structure-Activity Relationship Rheumatology HLA Antigens Electrochemistry medicine Humans Immunology and Allergy Pharmacology (medical) Amino Acid Sequence Binding selectivity Autoimmune disease chemistry.chemical_classification medicine.diagnostic_test HLA-DR Antigens Flow Cytometry medicine.disease Amino acid chemistry Biochemistry Peptides HLA-DRB1 Chains Protein Binding |
| Zdroj: | Arthritis & Rheumatism. 38:1744-1753 |
| ISSN: | 1529-0131 0004-3591 |
| DOI: | 10.1002/art.1780381207 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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