P2X7 purinergic receptor (P2X7R)

The **P2X7 purinergic receptor** is a trimeric, non-selective cation channel activated by high concentrations of extracellular adenosine triphosphate (ATP), far above physiological levels[1][7]. It consists of three subunits, each containing two transmembrane helices and a long extracellular domain forming the ATP binding site. Activation leads to cation flux (Ca²⁺, Na⁺, K⁺) through the channel, and sustained activation opens a pore allowing passage of larger organic molecules, which can trigger cell death[1][3][7]. The receptor plays a central role in immune response, inflammation, apoptosis, neurodegeneration, and various disease states. Multiple small-molecule antagonists have been developed, some of which bind uniquely allosteric sites making them highly selective[2][4][8]. The receptor's activity is finely modulated by splice variants, post-translational modifications (e.g., palmitoylation), and membrane protein interactions, making it a complex but attractive drug target[1][6]. The term "nfP2X7" does not correspond to any canonical classification and should be corrected to "P2X7 purinergic receptor".

Other names

P2X7 receptorP2X7RPurinergic receptor P2X, ligand-gated ion channel 7P2Z receptor (historical)Gene name: P2RX7

Antagonists bind to allosteric sites, blocking channel activation and pore formation Inhibitors prevent ATP-induced conformational changes and subsequent cell signaling, inflammation, and apoptosis