Table 2.
Ligand | Sequence | Kd / μM | ΔH / kcal.mol−1 | TΔS / kcal.mol−1 | ΔG / kcal.mol−1 |
---|---|---|---|---|---|
ErbB4 | 75 ± 8 | −5.58 ± 0.33 | +0.06 ± 0.39 | −5.64 ± 0.06 | |
p73 | 60 ± 6 | −7.33 ± 0.26 | −1.55 ± 0.33 | −5.78 ± 0.07 | |
PTCH1 | 79 ± 8 | −5.86 ± 0.54 | −0.25 ± 0.60 | −5.61 ± 0.06 | |
PTPN14 | 214 ± 30 | −4.69 ± 0.42 | +0.33 ± 0.51 | −5.02 ± 0.08 | |
SMAD7 | 53 ± 8 | −12.10 ± 0.57 | −6.25 ± 0.65 | −5.85 ± 0.09 | |
TMG2 | 84 ± 9 | −9.28 ± 0.41 | −3.71 ± 0.48 | −5.57 ± 0.07 | |
WBP1 | 141 ± 12 | −10.46 ± 0.76 | −5.20 ± 0.81 | −5.26 ± 0.05 | |
WBP2 | 42 ± 7 | −7.51 ± 0.68 | −1.53 ± 0.78 | −5.98 ± 0.10 |
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.