ArticleScientific reports2017
The low binding affinity of D-serine at the ionotropic glutamate receptor GluD2 can be attributed to the hinge region.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- Article
- Loss of activation by GABA in vertebrate delta ionotropic glutamate receptors.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- GluD receptors are functional ion channels.Biophysical journal · 2023Review
- Neuromechanobiology: An Expanding Field Driven by the Force of Greater Focus.Advanced healthcare materials · 2021Review
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Structural biology and thermodynamics of GluD receptors.Neuropharmacology · 2021Review
- D-Serine Potently Drives Ligand-Binding Domain Closure in the Ionotropic Glutamate Receptor GluD2.Structure (London, England : 1993) · 2020Article
- The structural bases for agonist diversity in anProceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Challenge of Interpreting Glutamate-Receptor Ion-Channel Structures.Biophysical journal · 2017Review
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Authors and funding
9 authors at 2 institutions in 2 countries.
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Abstract
Ionotropic glutamate receptors (iGluRs) are responsible for most of the fast excitatory communication between neurons in our brain. The GluD2 receptor is a puzzling member of the iGluR family: It is involved in synaptic plasticity, plays a role in human diseases, e.g. ataxia, binds glycine and D-serine with low affinity, yet no ligand has been discovered so far that can activate its ion channel. In this study, we show that the hinge region connecting the two subdomains of the GluD2 ligand-binding domain is responsible for the low affinity of D-serine, by analysing GluD2 mutants with electrophysiology, isothermal titration calorimetry and molecular dynamics calculations. The hinge region is highly variable among iGluRs and fine-tunes gating activity, suggesting that in GluD2 this region has evolved to only respond to micromolar concentrations of D-serine.
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