ArticleThe Journal of biological chemistry2010
Subunit arrangement in N-methyl-D-aspartate (NMDA) receptors.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 34 citations in OpenAlex.
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Article
- Conformational spread and dynamics in allostery of NMDA receptors.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Dissecting diverse functions of NMDA receptors by structural biology.Current opinion in structural biology · 2019Review
- Mapping the Conformational Landscape of Glutamate Receptors Using Single Molecule FRET.Trends in neurosciences · 2019Review
- NMDA Receptors in Astrocytes: In Search for Roles in Neurotransmission and Astrocytic Homeostasis.International journal of molecular sciences · 2019Review
- Stargazin Modulation of AMPA Receptors.Cell reports · 2016Article
- Structural rearrangement of the intracellular domains during AMPA receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Probing Intersubunit Interfaces in AMPA-subtype Ionotropic Glutamate Receptors.Scientific reports · 2016Article
- A conserved structural mechanism of NMDA receptor inhibition: A comparison of ifenprodil and zinc.The Journal of general physiology · 2015Article
- Conformational transitions in the glycine-bound GluN1 NMDA receptor LBD via single-molecule FRET.Biophysical journal · 2015Article
- Subtype-dependent N-methyl-D-aspartate receptor amino-terminal domain conformations and modulation by spermine.The Journal of biological chemistry · 2015Article
- Structure and gating of tetrameric glutamate receptors.The Journal of physiology · 2015Review
- The multifaceted subunit interfaces of ionotropic glutamate receptors.The Journal of physiology · 2015Review
- Molecular bases of NMDA receptor subtype-dependent properties.The Journal of physiology · 2015Review
- Single-molecule patch-clamp FRET microscopy studies of NMDA receptor ion channel dynamics in living cells: revealing the multiple conformational states associated with a channel at its electrical off state.Journal of the American Chemical Society · 2014Article
- Luminescence resonance energy transfer to study conformational changes in membrane proteins expressed in mammalian cells.Journal of visualized experiments : JoVE · 2014Article
- Proton-mediated conformational changes in an acid-sensing ion channel.The Journal of biological chemistry · 2013Article
- Amino-terminal domain tetramer organization and structural effects of zinc binding in the N-methyl-D-aspartate (NMDA) receptor.The Journal of biological chemistry · 2013Article
- α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) and N-methyl-D-aspartate (NMDA) receptors adopt different subunit arrangements.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
N-Methyl-d-aspartate (NMDA) receptors, the main mediators of excitatory synaptic transmission, are heterotetrameric receptors. Typically, glycine binding NR1 subunits co-assemble with glutamate binding NR2 subunits to form a functional receptor. Here we have used luminescence resonance energy transfer (LRET) investigations to establish the specific configuration in which these subunits assemble to form the functional tetramer and show that the dimer of dimers structure is formed by the NR1 subunits assembling diagonally to each other. The distances measured by LRET are consistent with the NMDA structure predicted based on cross-linking investigations and on the structure of the full-length alpha-amino-5-methyl-3-hydroxy-4-isoxazole propionic acid (AMPA) receptor structure (1). Additionally, the LRET distances between the NR1 and NR2A subunits within a dimer measured in the desensitized state of the receptor are longer than the distances in the previously published crystal structure of the isolated ligand binding domain of NR1-NR2A. Because the dimer interface in the isolated ligand binding domain crystallizes in the open channel structure, the longer LRET distances would be consistent with the decoupling of the dimer interface in the desensitized state. This is similar to what has been previously observed for the AMPA subtype of the ionotropic glutamate receptors, suggesting a similar mechanism for desensitization in the two subtypes of the glutamate receptor.
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