ArticleThe Journal of biological chemistry2011
Conformational changes at the agonist binding domain of the N-methyl-D-aspartic acid receptor.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 33 citations in OpenAlex.
- Comparative Analysis of Umami Substances and Potential Regulatory Genes in Six Economic Bivalves.Foods (Basel, Switzerland) · 2025Article
- Conformational equilibrium of an ABC transporter analyzed by luminescence resonance energy transfer.Biophysical journal · 2025Article
- Structural insights into NMDA receptor pharmacology.Biochemical Society transactions · 2023Review
- CaCommunications biology · 2023Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Activation and desensitization of ionotropic glutamate receptors by selectively triggering pre-existing motions.Neuroscience letters · 2019Review
- 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
- The structure-energy landscape of NMDA receptor gating.Nature chemical biology · 2017Article
- NMDA receptors: linking physiological output to biophysical operation.Nature reviews. Neuroscience · 2017Review
- Stargazin Modulation of AMPA Receptors.Cell reports · 2016Article
- Conformational Selection and Submillisecond Dynamics of the Ligand-binding Domain of the N-Methyl-d-aspartate Receptor.The Journal of biological chemistry · 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
- Subtype-dependent N-methyl-D-aspartate receptor amino-terminal domain conformations and modulation by spermine.The Journal of biological chemistry · 2015Article
- Structural dynamics of the glycine-binding domain of the N-methyl-D-aspartate receptor.The Journal of biological chemistry · 2015Article
- Stargazin promotes closure of the AMPA receptor ligand-binding domain.The Journal of general physiology · 2014Article
- Luminescence resonance energy transfer to study conformational changes in membrane proteins expressed in mammalian cells.Journal of visualized experiments : JoVE · 2014Article
- Functional analysis and regulation of purified connexin hemichannels.Frontiers in physiology · 2014Review
- 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
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The conformational changes in the agonist binding domain of the glycine-binding GluN1 and glutamate-binding GluN2A subunits of the N-methyl D-aspartic acid receptor upon binding agonists of varying efficacy have been investigated by luminescence resonance energy transfer (LRET) measurements. The LRET-based distances indicate a cleft closure conformational change at the GluN1 subunit upon binding agonists; however, no significant changes in the cleft closure are observed between partial and full agonists. This is consistent with the previously reported crystal structures for the isolated agonist binding domain of this receptor. Additionally, the LRET-based distances show that the agonist binding domain of the glutamate-binding GluN2A subunit exhibits a graded cleft closure with the extent of cleft closure being proportional to the extent of activation, indicating that the mechanism of activation in this subunit is similar to that of the glutamate binding α-amino-5-methyl-3-hydroxy-4-isoxazole propionate and kainate subtypes of the ionotropic glutamate receptors.
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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.