Long-range coupling in an allosteric receptor revealed by mutant cycle analysis
about
Gating Movement of Acetylcholine Receptor Caught by Plunge-FreezingBlockade of neuronal α7-nAChR by α-conotoxin ImI explained by computational scanning and energy calculationsUsing mutant cycle analysis to elucidate long-range functional coupling in allosteric receptors.An improved ivermectin-activated chloride channel receptor for inhibiting electrical activity in defined neuronal populationsRegulation of catch binding by allosteric transitions.A self-consistent approach for determining pairwise interactions that underlie channel activation.Subunit interfaces contribute differently to activation and allosteric modulation of neuronal nicotinic acetylcholine receptors.NbIT--a new information theory-based analysis of allosteric mechanisms reveals residues that underlie function in the leucine transporter LeuT.A coupled array of noncovalent interactions impacts the function of the 5-HT3A serotonin receptor in an agonist-specific way.Free-energy relationships in ion channels activated by voltage and ligand.Binding interactions with the complementary subunit of nicotinic receptors.An engineered glutamate-gated chloride (GluCl) channel for sensitive, consistent neuronal silencing by ivermectin.Propofol modulation of α1 glycine receptors does not require a structural transition at adjacent subunits that is crucial to agonist-induced activationProbing the role of backbone hydrogen bonding in a critical beta sheet of the extracellular domain of a cys-loop receptor.Differential Contribution of Subunit Interfaces to α9α10 Nicotinic Acetylcholine Receptor Function.An Update on GABAρ Receptors.Heterologous expression and nonsense suppression provide insights into agonist behavior at α6β2 nicotinic acetylcholine receptors.Probing the non-canonical interface for agonist interaction with an α5 containing nicotinic acetylcholine receptor.Detection of native-state nonadditivity in double mutant cycles via hydrogen exchange.An Unaltered Orthosteric Site and a Network of Long-Range Allosteric Interactions for PNU-120596 in α7 Nicotinic Acetylcholine Receptors.Packing of the extracellular domain hydrophobic core has evolved to facilitate pentameric ligand-gated ion channel function.A triad of residues is functionally transferrable between 5-HT3 serotonin receptors and nicotinic acetylcholine receptors.Binding site opening by loop C shift and chloride ion-pore interaction in the GABAA receptor model.
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Long-range coupling in an allosteric receptor revealed by mutant cycle analysis
description
article científic
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article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on April 2009
@en
vedecký článok
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vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Long-range coupling in an allosteric receptor revealed by mutant cycle analysis
@en
Long-range coupling in an allosteric receptor revealed by mutant cycle analysis.
@nl
type
label
Long-range coupling in an allosteric receptor revealed by mutant cycle analysis
@en
Long-range coupling in an allosteric receptor revealed by mutant cycle analysis.
@nl
prefLabel
Long-range coupling in an allosteric receptor revealed by mutant cycle analysis
@en
Long-range coupling in an allosteric receptor revealed by mutant cycle analysis.
@nl
P2093
P2860
P1433
P1476
Long-range coupling in an allosteric receptor revealed by mutant cycle analysis
@en
P2093
Dennis A Dougherty
Kristin R Gleitsman
Shawnalea J Frazier
P2860
P304
P356
10.1016/J.BPJ.2008.12.3949
P407
P577
2009-04-01T00:00:00Z