ArticleBiophysical journal2013
Nicotinic receptor transduction zone: invariant arginine couples to multiple electron-rich residues.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Key role of the TM2-TM3 loop in calcium potentiation of the α9α10 nicotinic acetylcholine receptor.Cellular and molecular life sciences : CMLS · 2024Article
- Novel interplay between agonist and calcium binding sites modulates drug potentiation of α7 acetylcholine receptor.Cellular and molecular life sciences : CMLS · 2024Article
- Structural bases for stoichiometry-selective calcium potentiation of a neuronal nicotinic receptor.British journal of pharmacology · 2024Article
- A release of local subunit conformational heterogeneity underlies gating in a muscle nicotinic acetylcholine receptor.Nature communications · 2024Article
- Article
- Unmasking coupling between channel gating and ion permeation in the muscle nicotinic receptor.eLife · 2021Article
- Loss of Choline Agonism in the Inner Ear Hair Cell Nicotinic Acetylcholine Receptor Linked to the α10 Subunit.Frontiers in molecular neuroscience · 2021Article
- Structure, Function and Physiology of 5-Hydroxytryptamine Receptors Subtype 3.Sub-cellular biochemistry · 2021Review
- Mechanism of calcium potentiation of the α7 nicotinic acetylcholine receptor.The Journal of general physiology · 2020Article
- Understanding structure-function relationships of the human neuronal acetylcholine receptor: insights from the first crystal structures of neuronal subunits.British journal of pharmacology · 2018Review
- Full and partial agonists evoke distinct structural changes in opening the muscle acetylcholine receptor channel.The Journal of general physiology · 2018Article
- Mutations causing congenital myasthenia reveal principal coupling pathway in the acetylcholine receptor ε-subunit.JCI insight · 2018Article
- Mutational Analysis at Intersubunit Interfaces of an Anionic Glutamate Receptor Reveals a Key Interaction Important for Channel Gating by Ivermectin.Frontiers in molecular neuroscience · 2017Article
- Crystal structure of a human neuronal nAChR extracellular domain in pentameric assembly: Ligand-bound α2 homopentamer.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Improved resolution of single channel dwell times reveals mechanisms of binding, priming, and gating in muscle AChR.The Journal of general physiology · 2016Article
- Investigation of Congenital Myasthenia Reveals Functional Asymmetry of Invariant Acetylcholine Receptor (AChR) Cys-loop Aspartates.The Journal of biological chemistry · 2016Article
- Crystal structures of free and antagonist-bound states of human α9 nicotinic receptor extracellular domain.Nature structural & molecular biology · 2014Article
- Article
- Site-directed spin labeling reveals pentameric ligand-gated ion channel gating motions.PLoS biology · 2013Article
- Loop C and the mechanism of acetylcholine receptor-channel gating.The Journal of general physiology · 2013Article
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Authors and funding
2 authors.
Funding
Abstract
Gating of the muscle-type acetylcholine receptor (AChR) channel depends on communication between the ACh-binding site and the remote ion channel. A key region for this communication is located within the structural transition zone between the ligand-binding and pore domains. Here, stemming from β-strand 10 of the binding domain, the invariant αArg209 lodges within the hydrophobic interior of the subunit and is essential for rapid and efficient channel gating. Previous charge-reversal experiments showed that the contribution of αArg209 to channel gating depends strongly on αGlu45, also within this region. Here we determine whether the contribution of αArg209 to channel gating depends on additional anionic or electron-rich residues in this region. Also, to reconcile diverging findings in the literature, we compare the dependence of αArg209 on αGlu45 in AChRs from different species, and compare the full agonist ACh with the weak agonist choline. Our findings reveal that the contribution of αArg209 to channel gating depends on additional nearby electron-rich residues, consistent with both electrostatic and steric contributions. Furthermore, αArg209 and αGlu45 show a strong interdependence in both human and mouse AChRs, whereas the functional consequences of the mutation αE45R depend on the agonist. The emerging picture shows a multifaceted network of interdependent residues that are required for communication between the ligand-binding and pore domains.
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