ArticleProceedings of the National Academy of Sciences of the United States of America2011
Preferential use of unobstructed lateral portals as the access route to the pore of human ATP-gated ion channels (P2X receptors).
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed.
- Structural basis for a central permeation pathway in the P2X1 receptor.Cell discovery · 2026Article
- Mechanisms of ligand recognition and channel opening for P2X2 receptors in lipid nanodiscs.Science advances · 2026Article
- Mechanisms of ligand recognition and channel opening for P2X2 receptors in lipid nanodiscs.bioRxiv : the preprint server for biology · 2025Article
- P2XScience advances · 2024Article
- Two serial filters control P2X7 cation selectivity, Ser342 in the central pore and lateral acidic residues at the cytoplasmic interface.PNAS nexus · 2024Article
- Dilation of ion selectivity filters in cation channels.Trends in biochemical sciences · 2024Review
- Article
- Lateral fenestrations in the extracellular domain of the glycine receptor contribute to the main chloride permeation pathway.Science advances · 2022Article
- Accessibility of ENaC extracellular domain central core residues.The Journal of biological chemistry · 2022Article
- Molecular Pharmacology of P2X Receptors: Exploring Druggable Domains Revealed by Structural Biology.Frontiers in pharmacology · 2022Review
- Using Whole-Cell Electrophysiology and Patch-Clamp Photometry to Characterize P2X7 Receptor Currents.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Role of Conserved Residues and F322 in the Extracellular Vestibule of the Rat P2X7 Receptor in Its Expression, Function and Dye Uptake Ability.International journal of molecular sciences · 2020Article
- Altered allostery of the left flipper domain underlies the weak ATP response of rat P2X5 receptors.The Journal of biological chemistry · 2019Article
- Bile acids inhibit human purinergic receptor P2X4 in a heterologous expression system.The Journal of general physiology · 2019Article
- Mapping a novel positive allosteric modulator binding site in the central vestibule region of human P2X7.Scientific reports · 2019Article
- Simulation of P2X-mediated calcium signalling in microglia.The Journal of physiology · 2019Article
- Cystic fibrosis transmembrane conductance regulator (CFTR): Making an ion channel out of an active transporter structure.Channels (Austin, Tex.) · 2018Review
- Intersubunit physical couplings fostered by the left flipper domain facilitate channel opening of P2X4 receptors.The Journal of biological chemistry · 2017Article
- P2X4 ReceptorFrontiers in pharmacology · 2017Article
- P2X4 Receptor Function in the Nervous System and Current Breakthroughs in Pharmacology.Frontiers in pharmacology · 2017Review
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Authors and funding
4 authors.
Funding
Abstract
P2X receptors are trimeric cation channels with widespread roles in health and disease. The recent crystal structure of a P2X4 receptor provides a 3D view of their topology and architecture. A key unresolved issue is how ions gain access to the pore, because the structure reveals two different pathways within the extracellular domain. One of these is the central pathway spanning the entire length of the extracellular domain and covering a distance of ≈70 Å. The second consists of three lateral portals, adjacent to the membrane and connected to the transmembrane pore by short tunnels. Here, we demonstrate the preferential use of the lateral portals. Owing to their favorable diameters and equivalent spacing, the lateral portals split the task of ion supply threefold and minimize an ion's diffusive path before it succumbs to transmembrane electrochemical gradients.
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