Table 5.
Ligand | Sequence | Kd / µM | ΔH / kcal.mol−1 | TΔS / kcal.mol−1 | ΔG / kcal.mol−1 | ΔCp / cal.mol−1.K−1 |
---|---|---|---|---|---|---|
ErbB4 | 72 ± 13 | −13.55 ± 0.92 | −7.89 ± 1.02 | −5.66 ± 0.11 | −52 ± 8 | |
LATS1 | 32 ± 6 | −9.67 ± 0.28 | −3.51 ± 0.41 | −6.15 ± 0.12 | −5 ± 3 | |
p73 | 108 ± 10 | −10.70 ± 0.57 | −5.28 ± 0.62 | −5.42 ± 0.05 | −70 ± 42 | |
PTCH1 | 133 ± 12 | −13.95 ± 0.35 | −8.65 ± 0.30 | −5.30 ± 0.05 | −55 ± 7 | |
PTPN14 | 112 ± 8 | −19.70 ± 0.99 | −14.30 ± 1.03 | −5.40 ± 0.04 | −48 ± 11 | |
RUNX1 | 98 ± 12 | −18.00 ± 0.57 | −12.52 ± 0.64 | −5.48 ± 0.07 | −53 ± 25 | |
SMAD7 | 129 ± 8 | −16.40 ± 0.57 | −11.09 ± 0.60 | −5.31 ± 0.04 | −38 ± 32 | |
TMG2 | 120 ± 16 | −17.75 ± 0.49 | −12.39 ± 0.41 | −5.36 ± 0.08 | −45 ± 21 | |
WBP1 | 232 ± 33 | −17.55 ± 1.48 | −12.58 ± 1.57 | −4.97 ± 0.09 | −100 ± 28 | |
WBP2 | 132 ± 13 | −13.35 ± 0.64 | −8.05 ± 0.70 | −5.30 ± 0.06 | −90 ± 71 |
Note that in the wildtype WW1-WW2 tandem module, both WW domains are capable of ligand binding. 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. All binding stoichiometries were fixed to 2. Errors were calculated from at least three independent measurements to one standard deviation.