ArticleBiophysical journal2002
Modeling of the pore domain of the GLUR1 channel: homology with K+ channel and binding of channel blockers.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- The diversity of AMPA receptor inhibition mechanisms among amidine-containing compounds.Frontiers in pharmacology · 2024Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Screening for Activity Against AMPA Receptors Among Anticonvulsants-Focus on Phenytoin.Frontiers in pharmacology · 2021Article
- The lipophilic bullet hits the targets: medicinal chemistry of adamantane derivatives.Chemical reviews · 2013Review
- Open-channel blockade is less effective on GluN3B than GluN3A subunit-containing NMDA receptors.European journal of pharmacology · 2012Article
- A single GluN2 subunit residue controls NMDA receptor channel properties via intersubunit interaction.Nature neuroscience · 2012Article
- Glutamate receptor ion channels: structure, regulation, and function.Pharmacological reviews · 2010Review
- Common binding site for externally and internally applied AMPA receptor channel blockers.Journal of molecular neuroscience : MN · 2009Article
- KvAP-based model of the pore region of shaker potassium channel is consistent with cadmium- and ligand-binding experiments.Biophysical journal · 2005Article
- The molecular pharmacology and cell biology of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors.Pharmacological reviews · 2005Review
- Modeling P-loops domain of sodium channel: homology with potassium channels and interaction with ligands.Biophysical journal · 2005Article
- Modeling noncompetitive antagonism of a nicotinic acetylcholine receptor.Biophysical journal · 2004Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molecular models of the M2 segments of the GluR1 channel have been elaborated using a molecular mechanics approach. The models are based on the homology between pore-lining segments of AMPA receptor channels and the KcsA K+ channel and on cyclic H bonds at the Q/R site of the AMPA receptor channel. The N-terminal region of an M2 segment of the channel is assumed, like that of the K+ channel, to adopt a helical conformation. Due to a deletion, the C-terminal end of the M2 segment of the AMPA receptor is more stretched than that of the K+ channel. As a result, only a single oxygen ring may be exposed to the AMPA receptor channel pore. Data on the block of AMPA receptor channels by dicationic adamantane derivatives have been used to select the most relevant model. The model with the oxygen of a Gly residue (position +2 from the Q/R site) exposed to the pore best fits the experimental data. This model also fits experimental data for another class of AMPA receptor antagonists, the polyamine amides. According to the model, the side-chains of the C-terminal residues are involved in intra-receptor interactions that stabilize the structure of the channel rather than in interactions with ions in the pore.
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