ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2007
Cysteine substitution mutants give structural insight and identify ATP binding and activation sites at P2X receptors.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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38 citing papers in PubMed, 59 citations in OpenAlex.
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- 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
- Drosophila taste neurons as an agonist-screening platform for P2X receptors.Scientific reports · 2020Article
- Identification of a distinct desensitisation gate in the ATP-gated P2X2 receptor.Biochemical and biophysical research communications · 2020Article
- Organization of ATP-gated P2X1 receptor intracellular termini in apo and desensitized states.The Journal of general physiology · 2019Article
- Mapping the binding site of the P2X receptor antagonist PPADS reveals the importance of orthosteric site charge and the cysteine-rich head region.The Journal of biological chemistry · 2018Article
- Key sites for P2X receptor function and multimerization: overview of mutagenesis studies on a structural basis.Current medicinal chemistry · 2015Review
- Regulation of ATP-gated P2X channels: from redox signaling to interactions with other proteins.Antioxidants & redox signaling · 2014Review
- Article
- Principles and properties of ion flow in P2X receptors.Frontiers in cellular neuroscience · 2014Review
- Exploring the ATP-binding site of P2X receptors.Frontiers in cellular neuroscience · 2013Review
- Multiple roles of the extracellular vestibule amino acid residues in the function of the rat P2X4 receptor.PloS one · 2013Article
- Mass spectrometry analysis of human P2X1 receptors; insight into phosphorylation, modelling and conformational changes.Journal of neurochemistry · 2012Article
- A mechanism of intracellular P2X receptor activation.The Journal of biological chemistry · 2012Article
- Involvement of the cysteine-rich head domain in activation and desensitization of the P2X1 receptor.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Article
- Agonist binding evokes extensive conformational changes in the extracellular domain of the ATP-gated human P2X1 receptor ion channel.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Article
- Expression, purification, electron microscopy, N-glycosylation mutagenesis and molecular modeling of human P2X4 and Dictyostelium discoideum P2XA.Biochimica et biophysica acta · 2011Article
- Activation and regulation of purinergic P2X receptor channels.Pharmacological reviews · 2011Review
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2 authors at 1 institution in 1 country.
Funding
Abstract
P2X receptors for extracellular ATP are a distinct family of ligand-gated cation channels involved in physiological processes ranging from synaptic transmission to muscle contraction. Common ATP binding motifs are absent from P2X receptors, and the extent of the agonist binding site is unclear. We used cysteine-scanning mutagenesis, radiolabeled 2-azido ATP binding, and methanethiosulfonate (MTS) compounds to identify amino acid residues involved in ATP binding and gating of the human P2X1 receptor. The pattern of MTSEA [(2-aminoethyl)methanethiosulfonate hydrobromide] biotinylation was also used to determine the accessibility of substituted cysteine residues and whether this changed on addition of ATP. Analysis of cysteine-substituted mutants of the last 44 amino acid residues (S286-I329) in the extracellular loop before the second transmembrane segment showed that N290, F291, R292, and K309 mutants had reduced ATP potency and 2-azido ATP binding. MTS reagents produced additional shifts in ATP potency at these residues, suggesting that they are directly involved in ATP binding; the effects were dependent on the charge of the MTS reagent at K309C; one explanation for this is that K309 interacts directly with the negatively charged phosphate of ATP. The remainder of the cysteine substitutions had little or no effect on ATP potency. However, at the mutants D316C, G321C, A323C, and I328C, MTS reagents did not change ATP potency but modified agonist-evoked responses, suggesting that this region may contribute to the gating of the channel.
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