Table 1. Thermodynamics of D-serine binding to wild-type GluD2-LBD, wild-type GluN1-LBD, the GluD2-LBD-(H)GluN1 hinge region mutant as well as GluD2-LBD binding site mutants determined by isothermal titration calorimetry.
| Protein | Kd (μM) | ΔH (kcal/mol) | −ΤΔS (kcal/mol) | N | na |
|---|---|---|---|---|---|
| T = 20 °C | |||||
| GluD2-LBDb | 893 | 3.1 | −7.2 | 1c | |
| GluN1-LBD | 0.7 ± 0.3d | −3.2 ± 0.8 | −5.0 ± 1.2 | 0.33 ± 0.02 | 3 |
| GluD2-LBD-(H)GluN1 | 5.4 ± 1.7 | −4.3 ± 0.6 | −2.7 ± 0.8 | 0.79 ± 0.10 | 3 |
| T = 25 °C | |||||
| GluD2-LBD | 809 ± 4 | 3.1 ± 0.2 | −7.13 ± 0.05 | 1c | 3 |
| GluD2-LBD(Y496F) | 571 ± 115 | 1.4 ± 0.3 | −5.8 ± 0.3 | 1c | 3 |
| GluD2-LBD(Y543Q) | 790 ± 112 | 0.71 ± 0.06 | −5.00 ± 0.05 | 1c | 3 |
| GluD2-LBD(A686S) | 1090 ± 231 | 1.1 ± 0.1 | −5.11 ± 0.02 | 1c | 3 |
| GluD2-LBD(Y770F) | 117 ± 11 | −2.3 ± 0.1 | −2.8 ± 0.3 | 1c | 3 |
an = number of experiments.
bData from Naur et al.13.
cThe stoichiometry (N) was fixed at 1.
dStandard deviation given.