ArticleStructure (London, England : 1993)2007
The free energy landscapes governing conformational changes in a glutamate receptor ligand-binding domain.
Article in Structure (London, England : 1993), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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Who cites it
69 citing papers in PubMed, 117 citations in OpenAlex.
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- Arthropod repellent interactions with olfactory receptors and ionotropic receptors analyzed by molecular modeling.Current research in insect science · 2024Article
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- Exploration of phytoconstituents of Medhya Rasayana herbs to identify potential inhibitors forFrontiers in molecular biosciences · 2024Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Allosteric coupling of sub-millisecond clamshell motions in ionotropic glutamate receptor ligand-binding domains.Communications biology · 2021Article
- Structural biology and thermodynamics of GluD receptors.Neuropharmacology · 2021Review
- From bedside-to-bench: What disease-associated variants are teaching us about the NMDA receptor.The Journal of physiology · 2021Review
- Altered conformational sampling along an evolutionary trajectory changes the catalytic activity of an enzyme.Nature communications · 2020Article
- D-Serine Potently Drives Ligand-Binding Domain Closure in the Ionotropic Glutamate Receptor GluD2.Structure (London, England : 1993) · 2020Article
- Activation and desensitization of ionotropic glutamate receptors by selectively triggering pre-existing motions.Neuroscience letters · 2019Review
- Druggability Simulations and X-Ray Crystallography Reveal a Ligand-Binding Site in the GluA3 AMPA Receptor N-Terminal Domain.Structure (London, England : 1993) · 2019Article
- Mapping the Conformational Landscape of Glutamate Receptors Using Single Molecule FRET.Trends in neurosciences · 2019Review
- Population Shift Mechanism for Partial Agonism of AMPA Receptor.Biophysical journal · 2019Article
- High Conformational Variability in the GluK2 Kainate Receptor Ligand-Binding Domain.Structure (London, England : 1993) · 2019Article
- Article
- Article
- Energetics of Glutamate Binding to an Ionotropic Glutamate Receptor.The journal of physical chemistry. B · 2017Article
9 more citing papers are in PubMed but not listed here.
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2 authors at 1 institution in 1 country.
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Abstract
Ionotropic glutamate receptors are ligand-gated transmembrane ion channels activated by the binding of glutamate. The free energy landscapes governing the opening/closing of the GluR2 S1S2 ligand-binding domain in the apo, DNQX-, and glutamate-bound forms are computed by using all-atom molecular dynamics simulations with explicit solvent, in conjunction with an umbrella sampling strategy. The apo S1S2 easily accesses low-energy conformations that are more open than observed in X-ray crystal structures. A free energy of 9-12 kcal/mol becomes available upon glutamate binding for driving conformational changes in S1S2 associated with receptor activation. Small-angle X-ray scattering profiles calculated from computed ensemble averages agree better with experimental results than profiles calculated from static X-ray crystal structures. Water molecules in the cleft may contribute to stabilizing the apo S1S2 in open conformations. Free energy landscapes were also computed for the glutamate-bound T686A and T686S S1S2 mutants, and the results elaborate on findings from experimental functional studies.
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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.