Search results for "MESH: Protein Multimerization"

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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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