TABLE 1.

Binding and kinetic properties of HLA-DR1-peptide complexes formed with HLA-A2(104–117)-derived peptide mutants

^a Peptides are named with the substituted anchor residues.

^b The pockets 1, 4, 6, and 9 anchor residues in wild type peptides (WT) and corresponding substituted anchor residues are highlighted in bold and underlined. W1_N-me represented peptide with N-methylated tryptophan in pocket 1.

^c 50% inhibition concentration calculated from binding competition curves.

^d Intrinsic dissociation half-life calculated from the dissociation curves.

^e DM-mediated dissociation half-life measured in the presence of 0.5 μm DM calculated from the dissociation curves.

^f DM susceptibility, which was calculated as the specific increase in dissociation rate in the presence of DM (k_{off, DM} − k_{off, in})/[DM], where [DM] = 0.5 μm.