Introduction of P2RX3
P2X purinoceptor 3 (P2RX3) is encoded by human P2RX3 gene, which is mapped to chromosome 11q12.1. P2RX3 is composed of 397 amino acids with a molecular weight of 44 kD. The structure of P2RX3 is predicted to contain 2 short intracellular domains, 2 transmembrane-spanning regions, and a large extracellular domain. P2RX3 subunit shares 43% and 47% identity with P2RX1 and P2RX2, respectively. In addition, 10 cysteine residues are conserved in P2RX3, so that tertiary structures may also be conserved. P2RX3 has a biased expression in heart and testis.
|Basic Information of P2RX3|
|Protein Name||P2X purinoceptor 3|
|Aliases||ATP receptor, Purinergic receptor, P2X3|
|Organism||Homo sapiens (Human)|
Function of P2RX3 Membrane Protein
P2RX3 is an important member of P2X receptors family, which function as extracellular ATP-gated cation channels to play roles in many physiological and pathological processes, including synaptic transmissions, hearing, thrombosis, pain perception, hypertension, immune regulation, etc. P2RX3 is reported to involve in blood coagulation, peristalsis, regulation of synaptic plasticity, sensory perception of taste, regulation of calcium-mediated signaling, neuromuscular synaptic transmission, and so on. Data show that P2RX3 has an extremely tight association with ASIC3 to form a pain-relevant and ligand-gated cationic channel, resulting in unilateral depression of P2RX3 currents and switch of ionic conductance. P2RX3 deficiency in mice is involved in urinary bladder hyporeflexia and reduced pain-related behavior. It is documented that P2X3 is up-regulated during the stretch of bladder urothelial cells from patients with interstitial cystitis, indicating that P2X3 may represent a selective therapeutic target for overactive bladder.
Fig.1 Crystal structure of the ATP-gated human P2RX3 ion channel. (Mansoor, 2016)
Application of P2RX3 Membrane Protein in Literature
This article verifies the expression of P2RX3 in human carotid bodies and finds hyperactivity of carotid bodies in individuals with hypertension, suggesting that P2X3 receptor may be a potential new target for human hypertension therapy.
This article discovers several P2X3 receptor antagonists by structure-activity study, and one of them shows potent and specific analgesic efficacy and antagonistic activity.
This article indicates that the mechanism underlying the pain-relieving effects of gardenoside and ozone may be regulated by repression of P2RX7 and P2RX3 purine receptors in the DRG, suggesting that gardenoside and ozone may be potential drug candidates that target P2X7 and P2X3 purine receptors.
This report suggests that up-regulation of P2RX2 and P2RX3 receptors may possibly play a role in heroin withdrawal-induced hyperalgesia.
This article defines the molecular interactions between the receptors and drugs and the mechanism by which allosteric changes in the left flipper, dorsal fin, and lower body domains modulate ATP activation of P2X3, inspiring new strategies to develop P2X3-specific allosteric modulators for clinical use.
P2RX3 Preparation Options
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