ArticleStructure (London, England : 1993)2013
Anions mediate ligand binding in Adineta vaga glutamate receptor ion channels.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 18 citations in OpenAlex.
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- Evolution of iGluR ligand specificity, polyamine regulation, and ion selectivity inferred from a placozoan epsilon receptor.Communications biology · 2025Article
- The gating properties of Drosophila NMJ glutamate receptors and their dependence on Neto.The Journal of physiology · 2024Article
- Neto proteins differentially modulate the gating properties ofbioRxiv : the preprint server for biology · 2024Article
- Expression and Functional Analysis of Ctenophore Glutamate Receptor Genes.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Merging Signaling with Structure: Functions and Mechanisms of Plant Glutamate Receptor Ion Channels.Annual review of plant biology · 2023Review
- Structural insights into function of ionotropic glutamate receptors.Biochemistry (Moscow) Supplement. Series A, Membrane and cell biology · 2022Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Structure of the Arabidopsis thaliana glutamate receptor-like channel GLR3.4.Molecular cell · 2021Article
- Structure of the Arabidopsis Glutamate Receptor-like Channel GLR3.2 Ligand-Binding Domain.Structure (London, England : 1993) · 2021Article
- The structural bases for agonist diversity in anProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Glycine activated ion channel subunits encoded by ctenophore glutamate receptor genes.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Functional reconstitution of Drosophila melanogaster NMJ glutamate receptors.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Reduced curvature of ligand-binding domain free-energy surface underlies partial agonism at NMDA receptors.Structure (London, England : 1993) · 2015Article
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4 authors at 2 institutions in 2 countries.
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Abstract
AvGluR1, a glutamate receptor ion channel from the primitive eukaryote Adineta vaga, is activated by alanine, cysteine, methionine, and phenylalanine, which produce lectin-sensitive desensitizing responses like those to glutamate, aspartate, and serine. AvGluR1 LBD crystal structures reveal an unusual scheme for binding dissimilar ligands that may be utilized by distantly related odorant/chemosensory receptors. Arginine residues in domain 2 coordinate the γ-carboxyl group of glutamate, whereas in the alanine, methionine, and serine complexes a chloride ion acts as a surrogate ligand, replacing the γ-carboxyl group. Removal of Cl(-) lowers affinity for these ligands but not for glutamate or aspartate nor for phenylalanine, which occludes the anion binding site and binds with low affinity. AvGluR1 LBD crystal structures and sedimentation analysis also provide insights into the evolutionary link between prokaryotic and eukaryotic iGluRs and reveal features unique to both classes, emphasizing the need for additional structure-based studies on iGluR-ligand interactions.
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