ArticleThe EMBO journal1998
AMPA receptors and bacterial periplasmic amino acid-binding proteins share the ionic mechanism of ligand recognition.
Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 67 citations in OpenAlex.
- Molecular Dynamics Investigation of gluazo, a Photo-Switchable Ligand for the Glutamate Receptor GluK2.PloS one · 2015Article
- Glutamate, glutamate receptors, and downstream signaling pathways.International journal of biological sciences · 2013Review
- Glutamate receptor ion channels: structure, regulation, and function.Pharmacological reviews · 2010Review
- Ligand-free open-closed transitions of periplasmic binding proteins: the case of glutamine-binding protein.Biochemistry · 2010Article
- Agonist occupancy is essential for forward trafficking of AMPA receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
- Gating motions underlie AMPA receptor secretion from the endoplasmic reticulum.The EMBO journal · 2008Article
- AMPA receptor binding cleft mutations that alter affinity, efficacy, and recovery from desensitization.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2005Article
- Glutamate receptor trafficking: endoplasmic reticulum quality control involves ligand binding and receptor function.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2005Article
- Influence of a threonine residue in the S2 ligand binding domain in determining agonist potency and deactivation rate of recombinant NR1a/NR2D NMDA receptors.The Journal of physiology · 2004Article
- The N-methyl D-aspartate receptor glycine site and D-serine metabolism: an evolutionary perspective.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004Review
- Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core.The EMBO journal · 2003Article
- Amino-acid residues involved in glutamate receptor 6 kainate receptor gating and desensitization.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003Article
- Three-dimensional model of the extracellular domain of the type 4a metabotropic glutamate receptor: new insights into the activation process.Protein science : a publication of the Protein Society · 2000Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In order to identify key structural determinants for ligand recognition, we subjected the ligand-binding domain of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-selective glutamate receptor GluR-D subunit to site-directed mutagenesis. Based on the analysis of the [3H]AMPA-binding properties of the mutated binding sites, we constructed a revised three-dimensional model of the ligand-binding site, different in many respects from previously published models. In particular, our results indicate that the residues Arg507 and Glu727 represent the structural and functional correlates of Arg77 and Asp161 in the homologous bacterial lysine/ornithine/arginine-binding protein and histidine-binding protein, and directly interact with the alpha-carboxyl and alpha-amino group of the bound ligand, respectively. In contrast, Glu424, implicated previously in ionic interactions with the alpha-amino group of the agonist, is unlikely to have such a role in ligand binding. Our results indicate that glutamate receptors share with the bacterial polar amino acid-binding proteins the fundamental mechanism of amino acid recognition.
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