Extended Data Table 2.
Binding affinities for different P2Y12R constructs
| Inhibition of binding | Ki (nM), WT | Ki (nM), WT+BRIL | Ki (nM), WT+D294N mutation | Ki (nM), WT+BRIL +D294N mutation |
|---|---|---|---|---|
| ADP | 332±35 | 405±122 | 169±81 | 280±85 |
| 2MeSADP | 120±7.3 | 91.3±30.7 | 80.8±16.8 | 128±48 |
| 2MeSATP | 119±19.8 | 68.0±20.8 | 82.4±28.5 | 93.2±19.9 |
| AZD1283 | 31.5±11.9 | 39.3±9.9 | 42.2±27.7 | 43.9±10.0 |
| PSB-0739 | 275±58 | 155±73 | 72.8±16.7 † | 157±58 |
| Ticagrelor | 454±110 | 299±138 | 424±193 | 182±70 |
| Saturation binding | WT | WT+BRIL | WT+D294N mutation | WT+BRIL+D294N mutation |
|---|---|---|---|---|
| Kd (nM) | 35.9±6.3 | 36.7±3.6 | 33.6±10.2 | 51.5±12.0 |
| Bmax (pmol/mg protein) | 6.34±0.27 | 6.87±0.78 | 11.4+1.1 | 11.9±0.63 |
Data represent mean ± standard error of the mean (s.e.m.) from 3–8 separate experiments performed in duplicate.
†
One-way analysis of variance with post-hoc test yielded significant difference (P<0.05) compared with wild type (WT) but not with WT+BRIL and WT+BRIL+D294N groups (P>0.05). The affinities of other ligands at wild type are not significantly different from their affinities at mutants (P > 0.05).