| rP2X2 construct . | EC50 (µM) . | nH . | n . |
|---|---|---|---|
| WT | 32 ± 4 | 1.4 ± 0.1 | 15 |
| Thr184Ser | 26 ± 3 | 1.4 ± 0.1 | 25 |
| Thr184Val | 3,200 ± 200**** | 1.3 ± 0.1 | 14 |
| Ile185Val | 23 ± 3 | 1.3 ± 0.1 | 10 |
| Ile185Vah | 460 ± 20** | 1.3 ± 0.1 | 10 |
| Val96Vah | 27 ± 2 | 1.7 ± 0.1 | 6 |
| rP2X2 construct . | EC50 (µM) . | nH . | n . |
|---|---|---|---|
| WT | 32 ± 4 | 1.4 ± 0.1 | 15 |
| Thr184Ser | 26 ± 3 | 1.4 ± 0.1 | 25 |
| Thr184Val | 3,200 ± 200**** | 1.3 ± 0.1 | 14 |
| Ile185Val | 23 ± 3 | 1.3 ± 0.1 | 10 |
| Ile185Vah | 460 ± 20** | 1.3 ± 0.1 | 10 |
| Val96Vah | 27 ± 2 | 1.7 ± 0.1 | 6 |
ATP-elicited concentration–response data (EC50) and Hill coefficient (nH; shown as mean ± SEM), as well as number of experiments (n) for WT and Thr184/Ile185 mutants, including the Ile185Vah and Val96Vah amide-to-ester mutants (the latter served as a control for Vah incorporation). Significant differences were determined by one-way ANOVA with Dunnett’s test. **, P < 0.01; ****, P < 0.0001.