Table 1.
Binding energetics of peptide ligands to the hNEDD4-WW3, hYAP-WW1 and hYAP-WW2 domains.
| Ligand/sequence | WW domain | T (°C) | &Kd (μM) | &ΔHap (kJ mol−1) | ΔCp (kJ K−1 mol−1) |
|---|---|---|---|---|---|
|
p53bp2 EYPPYPP−3′P−2′PY0′PSG |
NEDD4-WW3 | 20 | 4.1 ± 0.2 | −45.6 ± 0.3 | −1.59 ± 0.01 |
| 25 | 5.3 ± 0.5 | −53.2 ± 0.7 | |||
| 30 | 9.1 ± 0.3 | −61.1 ± 0.6 | |||
| YAP-WW1 | 20 | 1.1 ± 0.5 | −54.8 ± 0.2 | −1,16 ± 0.06 | |
| 25 | 1.8 ± 0.1 | −61.1 ± 0.3 | |||
| 30 | 3.0 ± 0.1 | −66.4 ± 0.5 | |||
| YAP-WW2 | 20 | — | — | — | |
| 25 | 12.0 ± 0.6 | −57 ± 1 | |||
| 30 | — | — | |||
|
HTLV1 SDPQIP−3′P−2′PY0′VEP |
NEDD4-WW3 | 25 | 61 ± 1 | −68.2 ± 0.6 | — |
| YAP-WW1 | 25 | #308 ± 4 | — | ||
| YAP-WW2 | 25 | #260 ± 40 | — | ||
|
HTLV1 ter P−3′P−2′PY0′VEPTAP |
NEDD4-WW3 | 25 | 178 ± 3 | −74.0 ± 0.8 | — |
| YAP-WW1 | 25 | n. b. | — | ||
| YAP-WW2 | 25 | n. b. | — | ||
|
Ebola ILPTAP−3′P−2′EY0′MEA |
NEDD4-WW3 | 25 | 147 ± 4 | −50.7 ± 0.7 | — |
| YAP-WW1 | 25 | #750 ± 10 | — | ||
| YAP-WW2 | 25 | #560 ± 30 | — | ||
|
Ebola ter ILPTAP−3P−2′EY0′ |
NEDD4-WW3 | 25 | n. b. | — | — |
| YAP-WW1 | 25 | n. b. | — | ||
| YAP-WW2 | 25 | n. b. | — | ||
|
Marburg MQYLNP−3′P−2′PY0′ADH |
NEDD4-WW3 | 25 | 51 ± 1 | −73.2 ± 0.7 | — |
| YAP-WW1 | 25 | #67 ± 4 | — | ||
| YAP-WW2 | 25 | #17 ± 1 | — | ||
|
Rabies DLWLPP−3′P−2′EY0′VPL |
NEDD4-WW3 | 25 | 51 ± 1 | −65.8 ± 0.8 | — |
| YAP-WW1 | 25 | 181 ± 5 | −63.7 ± 0.9 | ||
| YAP-WW2 | 25 | n. b. | — | ||
|
PPPY P −3′ P −2′ PY 0′ |
NEDD4-WW3 | 25 | 210 ± 15 | *−38 ± 1 | — |
| YAP-WW1 | 25 | 320 ± 30 | *−39 ± 3 | ||
| YAP-WW2 | 25 | n. b. | — |
#Dissociation constants determined by titration experiments followed by fluorescence spectroscopy.
*Thermodynamic parameters obtained by ITC competitive experiments using the p53bp2 ligand.
n. b.: no binding.