ArticleThe Journal of biological chemistry2010
Gated access to the pore of a P2X receptor: structural implications for closed-open transitions.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 64 citations in OpenAlex.
- Two serial filters control P2X7 cation selectivity, Ser342 in the central pore and lateral acidic residues at the cytoplasmic interface.PNAS nexus · 2024Article
- How Structural Biology Has Directly Impacted Our Understanding of P2X Receptor Function and Gating.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Residues in Transmembrane Segments of the P2X4 Receptor Contribute to Channel Function and Ethanol Sensitivity.International journal of molecular sciences · 2020Article
- Identification of a distinct desensitisation gate in the ATP-gated P2X2 receptor.Biochemical and biophysical research communications · 2020Article
- CaThe Journal of biological chemistry · 2019Article
- Exploring conformational states and helical packings in the P2X receptor transmembrane domain by molecular dynamics simulation.Journal of biological physics · 2018Article
- New Insights Into Permeation of Large Cations Through ATP-Gated P2X Receptors.Frontiers in molecular neuroscience · 2018Article
- Localization of the gate and selectivity filter of the full-length P2X7 receptor.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Conductance of P2X4 purinergic receptor is determined by conformational equilibrium in the transmembrane region.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Photo-switchable tweezers illuminate pore-opening motions of an ATP-gated P2X ion channel.eLife · 2016Article
- Insights into the channel gating of P2X receptors from structures, dynamics and small molecules.Acta pharmacologica Sinica · 2016Review
- Article
- Roles of the lateral fenestration residues of the P2X₄ receptor that contribute to the channel function and the deactivation effect of ivermectin.Purinergic signalling · 2015Article
- Key sites for P2X receptor function and multimerization: overview of mutagenesis studies on a structural basis.Current medicinal chemistry · 2015Review
- Purinergic control of inflammation and thrombosis: Role of P2X1 receptors.Computational and structural biotechnology journal · 2015Review
- Structural and molecular modeling features of P2X receptors.International journal of molecular sciences · 2014Review
- Structural and functional properties of the rat P2X4 purinoreceptor extracellular vestibule during gating.Frontiers in cellular neuroscience · 2014Article
- Principles and properties of ion flow in P2X receptors.Frontiers in cellular neuroscience · 2014Review
- Post-translational regulation of P2X receptor channels: modulation by phospholipids.Frontiers in cellular neuroscience · 2013Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
P2X receptors are ligand-gated cation channels that transition from closed to open states upon binding ATP. The crystal structure of the closed zebrafish P2X4.1 receptor directly reveals that the ion-conducting pathway is formed by three transmembrane domain 2 (TM2) alpha-helices, each being provided by the three subunits of the trimer. However, the transitions in TM2 that accompany channel opening are incompletely understood and remain unresolved. In this study, we quantified gated access to Cd(2+) at substituted cysteines in TM2 of P2X2 receptors in the open and closed states. Our data for the closed state are consistent with the zebrafish P2X4.1 structure, with isoleucines and threonines (Ile-332 and Thr-336) positioned one helical turn apart lining the channel wall on approach to the gate. Our data for the open state reveal gated access to deeper parts of the pore (Thr-339, Val-343, Asp-349, and Leu-353), suggesting the closed channel gate is between Thr-336 and Thr-339. We also found unexpected interactions between native Cys-348 and D349C that result in tight Cd(2+) binding deep within the intracellular vestibule in the open state. Interpreted with a P2X2 receptor structural model of the closed state, our data suggest that the channel gate opens near Thr-336/Thr-339 and is accompanied by movement of the pore-lining regions, which narrow toward the cytosolic end of TM2 in the open state. Such transitions would relieve the barrier to ion flow and render the intracellular vestibule less splayed during channel opening in the presence of ATP.
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Registered trials
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.