Table 3.
P2X receptor structures solved to date. Structures are characterised by their conformation, bound ligands, resolution, method of determination and length of the construct
| Structure | Reference | Ligands’ bound and resolution | Receptor conformation | Method | Receptor construct |
|---|---|---|---|---|---|
| Zebrafish P2X4 receptor (zfP2X4) | [10, 92, 119] |
Apo 2.9–3.5 Å ATP 2.8 Å CTP 2.8 Å |
Closed, open | X-ray crystallography | Truncated |
| Rat P2X4 receptor (rP2X4) | [120] | N/A | N/A | NMR spectroscopy | Head domain |
| Gulf Coast tick P2X receptor (amP2X) | [121] | ATP + Zn2+ 2.9 Å | Pre-open | X-ray crystallography | Truncated |
| Human P2X3 receptor (hP2X3) | [89, 101, 94] |
Apo 3.0 Å ATP 2.8–2.9 Å 2MeSATP 3.1 Å TNP-ATP 3.3 Å A317491 3.1 Å Gefapixant 3.4 Å ATP + Mg2+ 3.8 Å ATP + Ca2+ 3.3 Å |
Open, closed, desensitised | X-ray crystallography | Truncated |
| Panda P2X7 receptor (pdP2X7) | [102] |
Apo 3.4 Å ATP + A804598 3.9 Å A740003 3.6 Å GW791343 3.3 Å JNJ47965567 3.2 Å AZ10606120 3.5 Å A804598 3.4 Å |
Closed | X-ray crystallography | Truncated |
| Chicken P2X7 receptor (ckP2X7) | [122] | TNP-ATP 3.1 Å | Closed | X-ray crystallography | Truncated |
| Rat P2X7 receptor (rP2X7) | [88] |
Apo 2.9 Å ATP 3.3 Å |
Closed, open | Cryo-EM | Full length |