Binding affinity independent contribution of peptide length to the stability of peptide-HLA-DR complexes in live antigen presenting cells

The effect of peptide length on the stability of peptide-HLR-DR1 (DR1) complexes was analyzed using two peptide series of increasing length, each containing a 7mer core with five DR1-binding anchors, extended stepwise with A1a residues at the N- and C-terminus, respectively. The A1a extensions, alth...

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Veröffentlicht in:	Human immunology 1998-08, Vol.59 (8), p.463-471
Hauptverfasser:	Siklodi, Botond, Vogt, Anne B, Kropshofer, Harald, Falcioni, Fiorenza, Molina, Margarita, Bolin, David R, Campbell, Robert, Hämmerling, Günter J, Nagy, Zoltan A
Format:	Artikel
Sprache:	eng
Schlagworte:	Antibodies, Monoclonal Antigen Presentation Antigen-Presenting Cells - immunology Binding Sites Cell Line, Transformed Half-Life Histocompatibility Antigens Class II HLA-D Antigens - immunology HLA-DR1 Antigen - metabolism Humans Lymphocyte Activation Oligopeptides - chemistry Oligopeptides - metabolism Peptide Fragments - chemistry T-Lymphocytes - immunology
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