ArticleThe Journal of biological chemistry2005
An intersubunit zinc binding site in rat P2X2 receptors.
Article in The Journal of biological chemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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The trial behind it
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Who cites it
55 citing papers in PubMed, 91 citations in OpenAlex.
- Copper Increases the Cooperative Gating of Rat P2X2a Receptor Channels.Pharmaceuticals (Basel, Switzerland) · 2024Article
- Identifiability of equilibrium constants for receptors with two to five binding sites.The Journal of general physiology · 2023Article
- The Function and Regulation of Zinc in the Brain.Neuroscience · 2021Review
- New Insights of the Zn(II)-Induced P2 × 4R Positive Allosteric Modulation: Role of Head Receptor Domain SS2/SS3, E160 and D170.International journal of molecular sciences · 2020Article
- P2X receptors.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016Review
- Zinc as Allosteric Ion Channel Modulator: Ionotropic Receptors as Metalloproteins.International journal of molecular sciences · 2016Review
- Inter-subunit disulfide locking of the human P2X3 receptor elucidates ectodomain movements associated with channel gating.Purinergic signalling · 2016Article
- Photo-switchable tweezers illuminate pore-opening motions of an ATP-gated P2X ion channel.eLife · 2016Article
- Key sites for P2X receptor function and multimerization: overview of mutagenesis studies on a structural basis.Current medicinal chemistry · 2015Review
- Conformational flexibility of the agonist binding jaw of the human P2X3 receptor is a prerequisite for channel opening.British journal of pharmacology · 2014Article
- Regulation of ATP-gated P2X channels: from redox signaling to interactions with other proteins.Antioxidants & redox signaling · 2014Review
- Signal transmission within the P2X2 trimeric receptor.The Journal of general physiology · 2014Article
- Ectodomain movements of an ATP-gated ion channel (P2X2 receptor) probed by disulfide locking.The Journal of biological chemistry · 2014Article
- Exploring the ATP-binding site of P2X receptors.Frontiers in cellular neuroscience · 2013Review
- Heteromeric assembly of P2X subunits.Frontiers in cellular neuroscience · 2013Review
- Inter- and intrasubunit interactions between transmembrane helices in the open state of P2X receptor channels.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- P2X receptor intermediate activation states have altered nucleotide selectivity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- P2X receptors as drug targets.Molecular pharmacology · 2013Review
- Functional identification of close proximity amino acid side chains within the transmembrane-spanning helixes of the P2X2 receptor.PloS one · 2013Article
- Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
P2X receptors are ATP-gated ion channels made up of three similar or identical subunits. It is unknown whether ligand binding is intersubunit or intrasubunit, either for agonists or for allosteric modulators. Zinc binds to rat P2X2 receptors and acts as an allosteric modulator, potentiating channel opening. To probe the location of this zinc binding site, P2X2 receptors bearing mutations of the histidines at positions 120 and 213 were expressed in Xenopus oocytes. Studies of H120C and H213C mutants produced five lines of evidence consistent with the hypothesis that the residues in these positions bind zinc. Mixing of subunits containing the H120A or H213A mutation generated receptors that showed zinc potentiation, even though neither of these mutant receptors showed zinc potentiation on its own. Furthermore, expression of trimeric concatamers with His --> Ala mutations at some but not all six positions showed that zinc potentiation correlated with the number of intersubunit histidine pairs. These results indicate that zinc potentiation requires an interaction across a subunit interface. Expression of the H120C/H213C double mutant resulted in the formation of ectopic disulfide bonds that could be detected by changes in the physiological properties of the receptors after treatment with reducing and oxidizing agents. Immunoblot analysis of H120C/H213C protein separated under nonreducing conditions demonstrated that the ectopic bonds were between adjacent subunits. Taken together, these data indicate that His120 and His213 sit close to each other across the interface between subunits and are likely to be key components of the zinc binding site in P2X2 receptors.
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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.