ArticleProceedings of the National Academy of Sciences of the United States of America2013
Glutamate receptor desensitization is mediated by changes in quaternary structure of the ligand binding domain.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 60 citations in OpenAlex.
- Structural and mechanistic insights into gating and allosteric modulation of GluN1-GluN3A NMDA receptors.Nature structural & molecular biology · 2026Article
- Mice carrying a GluN2B protein-truncating variant have altered NMDA receptor subunit composition and their behavior recapitulates patient phenotypes.Cellular and molecular life sciences : CMLS · 2026Article
- Structural insights into kainate receptor desensitization.Nature communications · 2025Article
- Structural basis of GluK2 kainate receptor activation by a partial agonist.Nature structural & molecular biology · 2025Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Structural Arrangement Produced by Concanavalin A Binding to Homomeric GluK2 Receptors.Membranes · 2021Article
- Article
- Structures of the archaerhodopsin-3 transporter reveal that disordering of internal water networks underpins receptor sensitization.Nature communications · 2021Article
- Molecular Crowding and Diffusion-Capture in Synapses.iScience · 2020Article
- Article
- The structural arrangement and dynamics of the heteromeric GluK2/GluK5 kainate receptor as determined by smFRET.Biochimica et biophysica acta. Biomembranes · 2020Article
- Neto proteins regulate gating of the kainate-type glutamate receptor GluK2 through two binding sites.The Journal of biological chemistry · 2019Article
- The structural arrangement at intersubunit interfaces in homomeric kainate receptors.Scientific reports · 2019Article
- The Challenge of Interpreting Glutamate-Receptor Ion-Channel Structures.Biophysical journal · 2017Review
- Article
- Configurational Preference of the Glutamate Receptor Ligand Binding Domain Dimers.Biophysical journal · 2017Article
- The structure and function of glutamate receptors: MgNeuropharmacology · 2017Review
- Structure and symmetry inform gating principles of ionotropic glutamate receptors.Neuropharmacology · 2017Review
- The dynamic AMPA receptor extracellular region: a platform for synaptic protein interactions.The Journal of physiology · 2016Review
- Article
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
Abstract
Glutamate receptor ion channels are membrane proteins that mediate excitatory synaptic transmission in the central nervous system of vertebrates. Insight into molecular mechanisms underlying glutamate receptor gating is limited by lack of structural information for receptors trapped in different conformational states. Here, we report the use of single-particle cryoelectron tomography to determine the structures, at ∼21 Å resolution, of full-length GluK2 kainate receptors trapped in antagonist-bound resting and agonist-bound desensitized states. The resting state, stabilized by the competitive antagonist LY466195, closely resembles the crystal structure of the AMPA receptor GluA2, with well-resolved proximal and distal subunits exhibiting cross-over between the twofold symmetric amino terminal domain and a twofold symmetric ligand binding domain (LBD) dimer of dimers assembly. In the desensitized state, the LBD undergoes a major rearrangement, resulting in a separation of the four subunits by ∼25 Å. However, the amino terminal domain, transmembrane, and cytoplasmic regions of the receptor have similar conformations in the resting and desensitized states. The LBD rearrangement was not anticipated in prior models based on crystal structures for soluble LBD dimer assemblies, and we speculate that subunit separation allows a better match to the fourfold symmetric ion channel domain. From fits of the amino terminal domain and LBD domains into the density map of the desensitized state we have derived a structural model for differences in quaternary conformation between the resting and desensitized states.
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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.