Structural diversity of human class II histocompatibility molecules induced by peptide ligands
- Georges, Bertrand
- Loing, Estelle
- Neveu, Raphaële
- Melnyk, Oleg
- Gras-Masse, Helene
- Auriault, Claude
DOIAbstract
AbstractSDS–PAGE analyses of stable HLA-DR1 complexes indicate that the binding of T cell epitopes can lead to multiple conformational variants. Whereas short T epitopes (<14-mer) induce complexes with apparent MW ranging from 47 to 57 kDa, longer peptides form generally high mobility complexes (44–45 kDa). The generation of HLA-DR1 conformational variants appears dependent on core peptide residues fitting inside the groove but can additionally be attributed to the presence of N- and C-terminal flanking residues (PFRs) acting as a complementary mechanism. These PFRs can jointly affect major histocompatibility complex class II conformation and stability, supporting the existence of alternative contacts at a distance from the classical bindin...
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