Table 1.
Ligand | Sequence | Kd / μM | ΔH / kcal.mol−1 | TΔS / kcal.mol−1 | ΔG / kcal.mol−1 |
---|---|---|---|---|---|
ErbB4 | 179 ± 10 | −7.85 ± 0.80 | −2.73 ± 0.83 | −5.12 ± 0.03 | |
p73 | 107 ± 9 | −16.65 ± 0.78 | −11.23 ± 0.82 | −5.42 ± 0.05 | |
PTCH1 | 278 ± 19 | −10.17 ± 0.62 | −5.31 ± 0.57 | −4.86 ± 0.04 | |
PTPN14 | 763 ± 62 | −5.96 ± 0.72 | −1.70 ± 0.77 | −4.26 ± 0.04 | |
SMAD7 | 272 ± 29 | −22.60 ± 0.99 | −17.73 ± 1.05 | −4.87 ± 0.06 | |
TMG2 | 202 ± 23 | −14.15 ± 0.49 | −9.10 ± 0.43 | −5.05 ± 0.07 | |
WBP1 | 368 ± 44 | −17.55 ± 0.78 | −12.86 ± 0.85 | −4.69 ± 0.07 | |
WBP2 | 133 ± 18 | −15.15 ± 0.49 | −9.85 ± 0.42 | −5.30 ± 0.08 |
The consensus residues within the PPXY motif of each peptide are colored red for clarity. All parameters were obtained from ITC measurements at 25°C and pH 7. Binding stoichiometries were fixed to unity to improve the accuracy of thermodynamic parameters. Errors were calculated from at least three independent measurements to one standard deviation.