Fig. 1: Affinity and kinetics of the interactions between tapasin and B44:02 and B44:05.
From: Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation
a SPR analyses of the interaction of biotinylated tapasin captured on a streptavidin chip and B44:02–9mer. b B44:05–9mer. c B44:05-T73C–6mer. Data are shown in red and fits of the data to a 1:1 binding model are overlaid in black. d equilibrium constant KD, e association rate constant ka and f dissociation rate constant kd. Kinetics data consisting of (n = 3) independent measurements of the same preparations of tapasin and MHC-I molecules of the indicated interactions are shown below each panel as mean and as scatter plots. p values, calculated by two-tailed unpaired t-test as implemented in GraphPad Prism, are indicated. These data are representative of similar measurements performed with multiple preparations over a span of two years. Source data are provided as a source data file.
