A Competitive Inhibitor Traps LeuT in an Open-to-Out Conformation
Singh SK, Piscitelli CL, Yamashita A, Gouaux E. A Competitive Inhibitor Traps LeuT in an Open-to-Out Conformation. Science 2008, 322: 1655-1661. PMID: 19074341, PMCID: PMC2832577, DOI: 10.1126/science.1166777.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid Transport SystemsAmino AcidsBacterial ProteinsBinding SitesBinding, CompetitiveBiological TransportCrystallizationCrystallography, X-RayHydrogen BondingHydrophobic and Hydrophilic InteractionsKineticsLeucineLigandsModels, BiologicalModels, MolecularProtein ConformationProtein Structure, TertiarySodiumSymportersTryptophanConceptsNeurotransmitter sodium symportersPrimary substrate siteAmino acid substratesSodium symportersSecondary transportersExtracellular gateSubstrate passageLeucine transporterArginine 30Substrate transportCellular membranesConformational changesAcid substratesConformational statesSubstrate siteFunctional studiesIon gradientsLeuTWeak binding sitesTransportersBinding sitesSmall moleculesCompetitive inhibitorConformationTrp complexLeuT: A prokaryotic stepping stone on the way to a eukaryotic neurotransmitter transporter structure
Singh SK. LeuT: A prokaryotic stepping stone on the way to a eukaryotic neurotransmitter transporter structure. Channels 2008, 2: 380-389. PMID: 19066470, DOI: 10.4161/chan.2.5.6904.Peer-Reviewed Original ResearchConceptsSodium binding siteSolute carrier 6 (SLC6) familyIntegral membrane proteinsStructure/function studiesBinding sitesCrystal structureEukaryotic counterpartsAccurate homology modelsTransporter structureBacterial membersMembrane proteinsNutrient uptakeSequence identityMolecular insightsConformational changesHomology modelSecondary transportLeuTNeurotransmitter clearanceLipid bilayersSolute moleculesBiochemical dataFunction studiesIon bindingCrucial role