P2RX3 Membrane Protein Introduction

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
Gene Name P2RX3
Aliases ATP receptor, Purinergic receptor, P2X3
Organism Homo sapiens (Human)
UniProt ID P56373
Transmembrane Times 2
Length (aa) 397

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.

Crystal structure of the ATP-gated human P2RX3 ion channel. Fig.1 Crystal structure of the ATP-gated human P2RX3 ion channel. (Mansoor, 2016)

Application of P2RX3 Membrane Protein in Literature

  1. Pijacka W., et al. Purinergic receptors in the carotid body as a new drug target for controlling hypertension. Nat Med. 2016, 22(10): 1151-1159. PubMed ID: 27595323

    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.

  2. Tobinaga H., et al. Pyrrolinone derivatives as a new class of P2X3 receptor antagonists. Part 1: Initial structure-activity relationship studies of a hit from a high throughput screening. Bioorg Med Chem Lett. 2018, 28(13): 2338-2342. PubMed ID: 29805055

    This article discovers several P2X3 receptor antagonists by structure-activity study, and one of them shows potent and specific analgesic efficacy and antagonistic activity.

  3. Yu M., et al. Gardenoside combined with ozone inhibits the expression of P2X3 and P2X7 purine receptors in rats with sciatic nerve injury. Mol Med Rep. 2018, 17(6): 7980-7986. PubMed ID: 29620177

    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.

  4. Leng C., et al. Upregulation of P2X2 and P2X3 receptors in rats with hyperalgesia induced by heroin withdrawal. Neuroreport. 2018, 29(8): 678-684. PubMed ID: 29596152

    This report suggests that up-regulation of P2RX2 and P2RX3 receptors may possibly play a role in heroin withdrawal-induced hyperalgesia.

  5. Wang J., et al. Druggable negative allosteric site of P2X3 receptors. Proc Natl Acad Sci U S A. 2018, 115(19): 4939-4944. PubMed ID: 29674445

    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

To obtain the soluble and functional target protein, we have developed the versatile Magic™ membrane protein production platform to provide high-quality membrane protein preparation service. Our experienced scientists will do their best to help you find a perfect match in your required formats. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-P2RX3 antibody development services.

Creative Biolabs has extensive experience to provide first-class membrane protein production service using a variety of strategies. Our highly professional scientists are confident to make your project a success. Based on our forward-looking research, rich technical force and highly cooperative group, we have successfully produced, purified, stabilized and characterized many challenging membrane protein targets for global customers. If you are interested in the service we can provide, please feel free to contact us for more information.


  1. Mansoor, et al. (2016). X-ray structures define human P2X3 receptor gating cycle and antagonist action. Nature. 538: 66-71.

All listed customized services & products are for research use only, not intended for pharmaceutical, diagnostic, therapeutic or any in vivo human use.

Online Inquiry

Verification code
Click image to refresh the verification code.


USA: 45-1 Ramsey Road, Shirley, NY 11967, USA
Europe: Heidenkampsweg 58, 20097 Hamburg, Germany
Call us at:
USA: 1-631-381-2994
Europe: 44-207-097-1828
Fax: 1-631-207-8356
Our customer service representatives are available 24 hours a day, 7 days a week. Contact Us