. Author manuscript; available in PMC: 2015 Dec 1.

Published in final edited form as: FEBS J. 2014 Nov 4;281(24):5532–5551. doi: 10.1111/febs.13095

Table 4.

Thermodynamic parameters for the binding of mutant WW1Y-WW2 tandem module of YAP2 to PPXY-containing peptides derived from various cognate ligands

Ligand	K_d / µM	ΔH / kcal.mol⁻¹	TΔS / kcal.mol⁻¹	ΔG / kcal.mol⁻¹	ΔC_p / cal.mol⁻¹.K⁻¹
ErbB4	129 ± 5	−14.95 ± 0.91	−9.64 ± 0.94	−5.31 ± 0.02	−65 ± 7
LATS1	68 ± 7	−11.40 ± 0.42	−5.71 ± 0.49	−5.69 ± 0.06	−27 ± 10
p73	134 ± 10	−13.65 ± 0.35	−8.36 ± 0.40	−5.29 ± 0.04	−53 ± 11
PTCH1	191 ± 7	−18.35 ± 0.49	−13.27 ± 0.52	−5.08 ± 0.02	−68 ± 11
PTPN14	103 ± 9	−21.70 ± 1.27	−16.25 ± 1.32	−5.44 ± 0.05	−75 ± 21
RUNX1	91 ± 10	−23.65 ± 0.64	−18.13 ± 0.70	−5.52 ± 0.06	−73 ± 18
SMAD7	387 ± 35	−28.70 ± 1.84	−24.03 ± 1.89	−4.66 ± 0.05	−40 ± 14
TMG2	148 ± 6	−24.1 ± 1.41	−18.87 ± 1.44	−5.23 ± 0.03	−48 ± 25
WBP1	361 ± 20	−28.35 ± 2.33	−23.65 ± 2.37	−4.70 ± 0.03	−80 ± 28
WBP2	190 ± 9	−17.50 ± 0.42	−12.41 ± 0.45	−5.08 ± 0.03	−50 ± 14

Note that the WW1Y-WW2 tandem module harbors W199Y mutation that abrogates ligand binding to WW1 domain. The consensus residues within the PPXY motif of each peptide are colored red for clarity. All parameters were obtained froms ITC measurements at 25°C and pH 7. All binding stoichiometries were fixed to unity. Errors were calculated from at least three independent measurements to one standard deviation.