ArticleThe Journal of biological chemistry2008
Molecular shape, architecture, and size of P2X4 receptors determined using fluorescence resonance energy transfer and electron microscopy.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 49 citations in OpenAlex.
- Identification of the molecular determinants of antagonist potency in the allosteric binding pocket of human P2X4.Frontiers in pharmacology · 2023Article
- Altered purinergic receptor expression in the frontal cortex in schizophrenia.Schizophrenia (Heidelberg, Germany) · 2022Article
- Identification of a novel P2X7 antagonist using structure-based virtual screening.Frontiers in pharmacology · 2022Article
- Residues in Transmembrane Segments of the P2X4 Receptor Contribute to Channel Function and Ethanol Sensitivity.International journal of molecular sciences · 2020Article
- Interaction of Purinergic P2X4 and P2X7 Receptor Subunits.Frontiers in pharmacology · 2017Article
- Article
- 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
- Imaging P2X4 receptor subcellular distribution, trafficking, and regulation using P2X4-pHluorin.The Journal of general physiology · 2014Article
- Heteromeric assembly of P2X subunits.Frontiers in cellular neuroscience · 2013Review
- Primitive ATP-activated P2X receptors: discovery, function and pharmacology.Frontiers in cellular neuroscience · 2013Review
- P2X receptor chimeras highlight roles of the amino terminus to partial agonist efficacy, the carboxyl terminus to recovery from desensitization, and independent regulation of channel transitions.The Journal of biological chemistry · 2013Article
- Molecular and functional properties of P2X receptors--recent progress and persisting challenges.Purinergic signalling · 2012Review
- Imaging P2X4 receptor lateral mobility in microglia: regulation by calcium and p38 MAPK.The Journal of biological chemistry · 2012Article
- 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
- Expression, purification, electron microscopy, N-glycosylation mutagenesis and molecular modeling of human P2X4 and Dictyostelium discoideum P2XA.Biochimica et biophysica acta · 2011Article
- Neuronal P2X2 receptors are mobile ATP sensors that explore the plasma membrane when activated.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Activation and regulation of purinergic P2X receptor channels.Pharmacological reviews · 2011Review
- P2X4 receptors interact with both P2X2 and P2X7 receptors in the form of homotrimers.British journal of pharmacology · 2011Article
- Structural interpretation of P2X receptor mutagenesis studies on drug action.British journal of pharmacology · 2010Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
P2X receptors are ATP-gated nonselective cation channels with important physiological roles. However, their structures are poorly understood. Here, we analyzed the architecture of P2X receptors using fluorescence resonance energy transfer (FRET) microscopy and direct structure determination using electron microscopy. FRET efficiency measurements indicated that the distance between the C-terminal tails of P2X(4) receptors was 5.6 nm. Single particle analysis of purified P2X(4) receptors was used to determine the three-dimensional structure at a resolution of 21A; the orientation of the particle with respect to the membrane was assigned by labeling the intracellular C termini with 1.8-nm gold particles and the carbohydrate-rich ectodomain with lectin. We found that human P2X(4) is a globular torpedo-like molecule with an approximate volume of 270 nm(3) and a compact propeller-shaped ectodomain. In this structure, the distance between the centers of the gold particles was 6.1 nm, which closely matches FRET data. Thus, our data provide the first views of the architecture, shape, and size of single P2X receptors, furthering our understanding of this important family of ligand-gated ion channels.
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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.