Table 1.
Dissociation constants of yeast-displayed T1 or interface mutants by flow cytometry
Yeast-displayed TCRs were titrated with monomeric MART-1·HLA-A2, as described in the legend to Fig. 8A. Resulting data were fit to a one-site-specific binding equation (Y = Bmax × X/(KD + X), where X is ligand concentration, and Y is mean fluorescence units) to obtain KD with GraphPad Prism software. Average KD values from several experiments (n = 7, 1, 2, 2, and 5 for T1, F91βY, F45βY/M97αR, F45βY/M97αQ/K41αA, and F45βY, respectively) are reported.
| Yeast-displayed TCR | KD |
|---|---|
| nm | |
| T1 | 101 ± 48 |
| F91βY | 122 ± 29 |
| F45βY/M97αR | 2.3 ± 0.3 |
| F45βY/M97αQ/K41αA | 1 ± 0.1 |
| F45βY | 2 ± 0.5 |