ArticleThe Journal of general physiology2004
Invariant aspartic Acid in muscle nicotinic receptor contributes selectively to the kinetics of agonist binding.
Article in The Journal of general physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 40 citations in OpenAlex.
- Origin of acetylcholine antagonism in ELIC, a bacterial pentameric ligand-gated ion channel.Communications biology · 2022Article
- 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
- Functional probes of drug-receptor interactions implicated by structural studies: Cys-loop receptors provide a fertile testing ground.Journal of medicinal chemistry · 2014Review
- Principles of agonist recognition in Cys-loop receptors.Frontiers in physiology · 2014Review
- Nicotinic receptor transduction zone: invariant arginine couples to multiple electron-rich residues.Biophysical journal · 2013Article
- Physostigmine and galanthamine bind in the presence of agonist at the canonical and noncanonical subunit interfaces of a nicotinic acetylcholine receptor.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Action of nicotine and analogs on acetylcholine receptors having mutations of transmitter-binding site residue αG153.The Journal of general physiology · 2013Article
- Unraveling subunit cooperativity in homotetrameric HCN2 channels.Biophysical journal · 2012Article
- A coupled array of noncovalent interactions impacts the function of the 5-HT3A serotonin receptor in an agonist-specific way.ACS chemical neuroscience · 2012Article
- End-plate acetylcholine receptor: structure, mechanism, pharmacology, and disease.Physiological reviews · 2012Review
- Synaptic neurotransmitter-gated receptors.Cold Spring Harbor perspectives in biology · 2012Review
- Probability fluxes and transition paths in a Markovian model describing complex subunit cooperativity in HCN2 channels.PLoS computational biology · 2012Article
- Glycine hinges with opposing actions at the acetylcholine receptor-channel transmitter binding site.Molecular pharmacology · 2011Article
- Disruption of an intersubunit electrostatic bond is a critical step in glycine receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- The positive allosteric modulator morantel binds at noncanonical subunit interfaces of neuronal nicotinic acetylcholine receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
- Detection and trapping of intermediate states priming nicotinic receptor channel opening.Nature · 2009Article
- Binding to gating transduction in nicotinic receptors: Cys-loop energetically couples to pre-M1 and M2-M3 regions.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
- Morantel allosterically enhances channel gating of neuronal nicotinic acetylcholine alpha 3 beta 2 receptors.Molecular pharmacology · 2008Article
- Nicotinic receptor interloop proline anchors beta1-beta2 and Cys loops in coupling agonist binding to channel gating.The Journal of general physiology · 2008Article
- Structural answers and persistent questions about how nicotinic receptors work.Frontiers in bioscience : a journal and virtual library · 2008Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We examined functional contributions of interdomain contacts within the nicotinic receptor ligand binding site using single channel kinetic analyses, site-directed mutagenesis, and a homology model of the major extracellular region. At the principal face of the binding site, the invariant alphaD89 forms a highly conserved interdomain contact near alphaT148, alphaW149, and alphaT150. Patch-clamp recordings show that the mutation alphaD89N markedly slows acetylcholine (ACh) binding to receptors in the resting closed state, but does not affect rates of channel opening and closing. Neither alphaT148L, alphaT150A, nor mutations at both positions substantially affects the kinetics of receptor activation, showing that hydroxyl side chains at these positions are not hydrogen bond donors for the strong acceptor alphaD89. However substituting a negative charge at alphaT148, but not at alphaT150, counteracts the effect of alphaD89N, demonstrating that a negative charge in the region of interdomain contact confers rapid association of ACh. Interpreted within the structural framework of ACh binding protein and a homology model of the receptor ligand binding site, these results implicate main chain amide groups in the domain harboring alphaW149 as principal hydrogen bond donors for alphaD89. The specific effect of alphaD89N on ACh association suggests that interdomain hydrogen bonding positions alphaW149 for optimal interaction with ACh.
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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.