Search results for " epibatidine"

showing 3 items of 3 documents

A possible desensitized state conformation of the human α7 nicotinic receptor: A molecular dynamics study

2017

International audience; The determination of the conformational states corresponding to diverse functional roles of ligand gated ion channels is subject of intense investigation with various techniques, from X-rays structure determination to electrophysiology and computational modeling. Even with a certain number of structures becoming recently available, only few major structural features distinguishing conductive open channel from the non conductive resting protein have been highlighted, while high-resolution details are still missing. The characterization of the desensitized conformation(s) is even more complex, and only few specific characteristics have been identified. Furthermore, exp…

0301 basic medicinealpha7 Nicotinic Acetylcholine ReceptorStereochemistryPyridinesBiophysicsMolecular Dynamics SimulationBiochemistry03 medical and health sciencesMolecular dynamicsmedicineHumansHomology modelingnicotinic receptor epibatidine molecular dynamics inactive stateIon channel[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]ChemistryProtein StabilityOrganic ChemistryHydrogen BondingBridged Bicyclo Compounds HeterocyclicSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Protein Structure Tertiary[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsElectrophysiology030104 developmental biologyNicotinic agonistα7 nicotinic receptorEpibatidineLigand-gated ion channel[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]medicine.drug
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A Structural Model of the Human α7 Nicotinic Receptor in an Open Conformation

2015

International audience; Nicotinic acetylcholine receptors (nAchRs) are ligand-gated ion channels that regulate chemical transmission at the neuromuscular junction. Structural information is available at low resolution from open and closed forms of an eukaryotic receptor, and at high resolution from other members of the same structural family, two prokaryotic orthologs and an eukary- otic GluCl channel. Structures of human channels however are still lacking. Homology modeling and Molecular Dynamics simulations are valuable tools to predict structures of unknown proteins, however, for the case of human nAchRs, they have been unsuccessful in providing a stable open structure so far. This is du…

Models MolecularHydrogen bondingalpha7 Nicotinic Acetylcholine ReceptorProtein ConformationMolecular Sequence DataMESH: Sequence Alignmentligand gated ion channles molecular dynamics simulation epibatidine waterlcsh:MedicineSequence alignmentMESH: Amino Acid SequenceMolecular Dynamics SimulationMESH: Models Molecular*Molecular dynamicsProtein structureSequence alignmentCationsHumansMESH: Molecular Dynamics SimulationHomology modelingAmino Acid SequenceNicotinic Receptorlcsh:ScienceBiochemical simulationsIon channelAcetylcholine receptorIonsMESH: Protein Conformation*MultidisciplinaryMESH: HumansMESH: Molecular Sequence DataChemistryMESH: Protein Multimerizationlcsh:RMESH: alpha7 Nicotinic Acetylcholine Receptor/chemistry*[SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]Transmembrane proteinSimulation and modelingNicotinic agonistBiochemistryBiophysicsProtein structurelcsh:QProtein MultimerizationResearch ArticleStructural Model
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Molecular dynamics simulations of a new model of human a7 nicotinic receptor

2014

human receptors epibatidine molecular dynamics simulations
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