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.
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.
Authors: Chu-Young Kim; Hanne Quarsten; Elin Bergseng; Chaitan Khosla; Ludvig M Sollid Journal: Proc Natl Acad Sci U S A Date: 2004-03-12 Impact factor: 11.205
Authors: A V Chervonsky; R M Medzhitov; L K Denzin; A K Barlow; A Y Rudensky; C A Janeway Journal: Proc Natl Acad Sci U S A Date: 1998-08-18 Impact factor: 11.205
Authors: Nadezda N Logunova; Christophe Viret; Leonid A Pobezinsky; Sara A Miller; Dmitri B Kazansky; John P Sundberg; Alexander V Chervonsky Journal: J Exp Med Date: 2005-07-04 Impact factor: 14.307