Search results for "Conotoxins"

showing 2 items of 2 documents

Closed-Locked and Apo-Resting State Structures of the Human α7 Nicotinic Receptor: A Computational Study

2018

International audience; Nicotinic acetylcholine receptors, belonging to the Cys-loop super-family of ligand-gated ion channels (LGICs), are membrane proteins present in neurons and at neuromuscular junctions. They are responsible for signal transmission, and their function is regulated by neurotransmitters, agonists and antagonists drugs. A detailed knowledge of their conformational transition in response to ligand binding is critical to understand the basis of ligand-receptor interaction, in view of new pharmacological approaches to control receptor activity. However, the scarcity of experimentally derived structures of human channels makes this perspective extremely challenging. To contri…

0301 basic medicinealpha7 Nicotinic Acetylcholine ReceptorProtein ConformationGeneral Chemical EngineeringMolecular Dynamics SimulationLibrary and Information Sciences03 medical and health sciencesMolecular dynamics0302 clinical medicineHumansHomology modelingReceptorIon channelAcetylcholine receptor[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]Protein StabilityChemistryWaterHydrogen BondingGeneral ChemistryLigand (biochemistry)molecular dynamicsComputer Science Applications[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsTransmembrane domain030104 developmental biologyNicotinic agonistBiophysics[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]Conotoxinsligand gated ion channel030217 neurology & neurosurgery
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α-Conotoxins EpI and AuIB switch subtype selectivity and activity in native versus recombinant nicotinic acetylcholine receptors

2003

The Xenopus laevis oocyte expression system was used to determine the activities of alpha-conotoxins EpI and the ribbon isomer of AuIB, on defined nicotinic acetylcholine receptors (nAChRs). In contrast to previous findings on intracardiac ganglion neurones, alpha-EpI showed no significant activity on oocyte-expressed alpha3beta4 and alpha3beta2 nAChRs but blocked the alpha7 nAChR with an IC50 value of 30 nM. A similar IC50 value (103 nM) was obtained on the alpha7/5HT3 chimeric receptor stably expressed in mammalian cells. Ribbon AuIB maintained its selectivity on oocyte-expressed alpha3beta4 receptors but unlike in native cells, where it was 10-fold more potent than native alpha-AuIB, had…

α7 nicotinic acetylcholine receptorα-Conotoxin AuIBRecombinant Fusion ProteinsBiophysicsXenopusNicotinic AntagonistsReceptors NicotinicPharmacologyTransfectionBiochemistrycomplex mixturesSubstrate SpecificityInhibitory Concentration 50Xenopus laevisStructural BiologyGeneticsmedicineAnimalsConotoxinNicotinic AntagonistReceptorMolecular BiologyAcetylcholine receptorbiologyα-Conotoxin EpICell Biologybiology.organism_classificationRatsCell biologyProtein SubunitsNicotinic acetylcholine receptorNicotinic agonistnervous systemIntracardiac gangliaOocytessense organsReceptors Serotonin 5-HT3ConotoxinsAcetylcholineXenopus laevis oocytemedicine.drugFEBS Letters
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