ArticleJournal of neurochemistry2009
Contribution of the region Glu181 to Val200 of the extracellular loop of the human P2X1 receptor to agonist binding and gating revealed using cysteine scanning mutagenesis.
Article in Journal of neurochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- Structural insights into the human P2X1 receptor and ligand interactions.Nature communications · 2024Article
- Drosophila taste neurons as an agonist-screening platform for P2X receptors.Scientific reports · 2020Article
- 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
- Mechanistic insights from resolving ligand-dependent kinetics of conformational changes at ATP-gated P2X1R ion channels.Scientific reports · 2016Article
- A Highly Conserved Salt Bridge Stabilizes the Kinked Conformation of β2,3-Sheet Essential for Channel Function of P2X4 Receptors.The Journal of biological chemistry · 2016Article
- Insights into the channel gating of P2X receptors from structures, dynamics and small molecules.Acta pharmacologica Sinica · 2016Review
- 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
- Structural and functional properties of the rat P2X4 purinoreceptor extracellular vestibule during gating.Frontiers in cellular neuroscience · 2014Article
- Exploring the ATP-binding site of P2X receptors.Frontiers in cellular neuroscience · 2013Review
- Heteromeric assembly of P2X subunits.Frontiers in cellular neuroscience · 2013Review
- Molecular and functional properties of P2X receptors--recent progress and persisting challenges.Purinergic signalling · 2012Review
- 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
- Molecular basis of selective antagonism of the P2X1 receptor for ATP by NF449 and suramin: contribution of basic amino acids in the cysteine-rich loop.British journal of pharmacology · 2012Article
- Pharmacochemistry of the platelet purinergic receptors.Purinergic signalling · 2011Article
- Cysteine scanning mutagenesis (residues Glu52-Gly96) of the human P2X1 receptor for ATP: mapping agonist binding and channel gating.The Journal of biological chemistry · 2011Article
- Agonist trapped in ATP-binding sites of the P2X2 receptor.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Allosteric modulation of ATP-gated P2X receptor channels.Reviews in the neurosciences · 2011Review
- Structural interpretation of P2X receptor mutagenesis studies on drug action.British journal of pharmacology · 2010Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
At the majority of mutants in the region Glu181-Val200 incorporating a conserved AsnPheThrPhiPhixLys motif cysteine substitution had no effect on sensitivity to ATP, partial agonists, or methanethiosulfonate (MTS) compounds. For the F185C mutant the efficacy of partial agonists was reduced by approximately 90% but there was no effect on ATP potency or the actions of MTS reagents. At T186C, F188C and K190C mutants ATP potency and partial agonists responses were reduced. The ATP sensitivity of the K190C mutant was rescued towards WT levels by positively charged (2-aminoethyl)methanethiosulfonate hydrobromide and reduced by negatively charged sodium (2-sulfonatoethyl) methanethiosulfonate. Both MTS reagents decreased ATP potency at the T186C mutant, and abolished responses at the F195C mutant. (32)P-2-azido ATP binding to the mutants T186C and K190C was sensitive to MTS reagents consistent with an effect on binding, however binding at F195C was unaffected indicating an effect on gating. The accessibility of the introduced cysteines was probed with (2-aminoethyl)methanethiosulfonate hydrobromide-biotin, this showed that the region Thr186-Ser192 is likely to form a beta sheet and that accessibility is blocked by ATP. Taken together these results suggest that Thr186, Phe188 and Lys190 are involved in ATP binding to the receptor and Phe185 and Phe195 contribute to agonist evoked conformational changes.
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