ArticleNature communications2023
Structural insights into the allosteric inhibition of P2X4 receptors.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 38 citations in OpenAlex.
- Chessboard Microneedle Array for Inflammation Regulation via Spatiotemporally Controlled Drug Delivery.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Structural basis for a central permeation pathway in the P2X1 receptor.Cell discovery · 2026Article
- Positive allosteric modulator activity of ginsenosides is restricted to P2X7 and P2X4 receptors.Purinergic signalling · 2026Article
- Cryo-EM structures of human P2X2/3 heteromer channel reveal the structural basis of ligand selectivity.Science advances · 2026Article
- Structure of the human P2X3 receptor reveals the basis for subtype-selective inhibition by sivopixant.PLoS biology · 2026Article
- Discovery of an allosteric binding site for anthraquinones at the human P2X4 receptor.Nature communications · 2025Article
- Bayesian inference of functional asymmetry in the homotrimeric ligand-gated ion channel P2XCommunications biology · 2025Article
- Understanding interspecies drug response variations between human and rodent P2X7 receptors.Nature communications · 2025Article
- P2RX4 promotes hepatocellular carcinoma progression via calcium-mediated PI3K/AKT activation and immune remodeling.World journal of surgical oncology · 2025Article
- Subtype-specific structural features of the hearing loss-associated human P2X2 receptor.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural basis of the multiple ligand binding mechanisms of the P2X1 receptor.Acta pharmacologica Sinica · 2025Article
- Analgesic Mechanism of Emodin in Neuropathic Pain Through Inhibiting P2X4 Purinoceptor Signaling.Molecular neurobiology · 2025Article
- Identification of New Human P2X7 Antagonists Using Ligand- and Structure-Based Virtual Screening.Journal of chemical information and modeling · 2025Article
- Species Differences of P2X4 Receptor Modulators.ACS pharmacology & translational science · 2025Article
- Towards P2X4 Positron Emission Tomography Tracing.Journal of medicinal chemistry · 2025Review
- Covalent-Allosteric Inhibitors: Do We Get the Best of Both Worlds?Journal of medicinal chemistry · 2025Review
- Human P2X4 receptor gating is modulated by a stable cytoplasmic cap and a unique allosteric pocket.Science advances · 2025Article
- Electrophysiology in neuropathic pain: a bibliometric analysis and literature review.Frontiers in neuroscience · 2025Review
- Mechanistic insights into Alpha-Synuclein binding to P2RX7: A molecular dynamic and docking study.PloS one · 2025Article
- Mechanistic insights into the selective targeting of P2X3 receptor by camlipixant antagonist.The Journal of biological chemistry · 2025Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
P2X receptors are ATP-activated cation channels, and the P2X4 subtype plays important roles in the immune system and the central nervous system, particularly in neuropathic pain. Therefore, P2X4 receptors are of increasing interest as potential drug targets. Here, we report the cryo-EM structures of the zebrafish P2X4 receptor in complex with two P2X4 subtype-specific antagonists, BX430 and BAY-1797. Both antagonists bind to the same allosteric site located at the subunit interface at the top of the extracellular domain. Structure-based mutational analysis by electrophysiology identified the important residues for the allosteric inhibition of both zebrafish and human P2X4 receptors. Structural comparison revealed the ligand-dependent structural rearrangement of the binding pocket to stabilize the binding of allosteric modulators, which in turn would prevent the structural changes of the extracellular domain associated with channel activation. Furthermore, comparison with the previously reported P2X structures of other subtypes provided mechanistic insights into subtype-specific allosteric inhibition.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.