ArticleJournal of structural biology2017
Structural modeling for the open state of an NMDA receptor.
Article in Journal of structural biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- Econeurobiology and brain development in children: key factors affecting development, behavioral outcomes, and school interventions.Frontiers in public health · 2024Review
- Different Forms of Disorder in NMDA-Sensitive Glutamate Receptor Cytoplasmic Domains Are Associated with Differences in Condensate Formation.Biomolecules · 2022Article
- Conformational rearrangement of the NMDA receptor amino-terminal domain during activation and allosteric modulation.Nature communications · 2021Article
- Correlated conformational dynamics of the human GluN1-GluN2A type N-methyl-D-aspartate (NMDA) receptor.Journal of molecular modeling · 2021Article
- NMDA Receptor Opening and Closing-Transitions of a Molecular Machine Revealed by Molecular Dynamics.Biomolecules · 2019Article
- Mapping the Conformational Landscape of Glutamate Receptors Using Single Molecule FRET.Trends in neurosciences · 2019Review
- An inter-dimer allosteric switch controls NMDA receptor activity.The EMBO journal · 2019Article
- A conserved glycine harboring disease-associated mutations permits NMDA receptor slow deactivation and high CaNature communications · 2018Article
- Computer Simulations Predict High Structural Heterogeneity of Functional State of NMDA Receptors.Biophysical journal · 2018Article
- Disease-associated missense mutations in GluN2B subunit alter NMDA receptor ligand binding and ion channel properties.Nature communications · 2018Article
- How does binding of agonist ligands control intrinsic molecular dynamics in human NMDA receptors?PloS one · 2018Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
NMDA receptors are tetrameric ligand-gated ion channels that are crucial for neurodevelopment and higher order processes such as learning and memory, and have been implicated in numerous neurological disorders. The lack of a structure for the channel open state has greatly hampered the understanding of the normal gating process and mechanisms of disease-associated mutations. Here we report the structural modeling for the open state of an NMDA receptor. Staring from the crystal structure of the closed state, we repacked the pore-lining helices to generate an initial open model. This model was modified to ensure tight packing between subunits and then refined by a molecular dynamics simulation in explicit membrane. We identify Cα-H…O hydrogen bonds, between the Cα of a conserved glycine in one transmembrane helix and a carbonyl oxygen of a membrane-parallel helix, at the extracellular side of the transmembrane domain as important for stabilizing the open state. This observation explains why mutations of the glycine are associated with neurological diseases and lead to significant decrease in channel open probability.
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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.