2014
Functionally Important Carboxyls in a Bacterial Homologue of the Vesicular Monoamine Transporter (VMAT)*
Yaffe D, Vergara-Jaque A, Shuster Y, Listov D, Meena S, Singh SK, Forrest LR, Schuldiner S. Functionally Important Carboxyls in a Bacterial Homologue of the Vesicular Monoamine Transporter (VMAT)*. Journal Of Biological Chemistry 2014, 289: 34229-34240. PMID: 25336661, PMCID: PMC4256354, DOI: 10.1074/jbc.m114.607366.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsArginineBacterial ProteinsBiogenic MonoaminesBrevibacillusCarrier ProteinsDrug Resistance, BacterialEscherichia coliEvolution, MolecularGene ExpressionHistidineModels, MolecularMolecular Sequence DataProtein FoldingRatsRecombinant ProteinsSequence AlignmentStructural Homology, ProteinStructure-Activity RelationshipSubstrate SpecificitySynaptic TransmissionVesicular Monoamine Transport ProteinsConceptsBacterial multidrug transportersMultidrug transporterBacterial homologueVesicular monoamine transporterRat vesicular monoamine transporterMonoamine transportersPreliminary biochemical characterizationMammalian transportersTransmembrane helicesMammalian counterpartsTransmembrane segmentsMammalian organismsEvolutionary aspectsMajor facilitatorBiochemical characterizationImportant carboxylB. brevisHomology modelBiochemical studiesTransportersHomologuesCarboxyl residuesAntibiotic resistanceOrganismsNeurotransporters
2009
Crystal structure and association behaviour of the GluR2 amino‐terminal domain
Jin R, Singh SK, Gu S, Furukawa H, Sobolevsky AI, Zhou J, Jin Y, Gouaux E. Crystal structure and association behaviour of the GluR2 amino‐terminal domain. The EMBO Journal 2009, 28: 1812-1823. PMID: 19461580, PMCID: PMC2699365, DOI: 10.1038/emboj.2009.140.Peer-Reviewed Original ResearchConceptsAmino-terminal domainLigand-gated ion channel proteinsReceptor assemblyModular domain architectureIon channel proteinsFast excitatory neurotransmissionSame subfamilyMolecular basisReceptor subfamiliesChannel proteinsMolecular processesSubfamiliesAMPA receptor GluR1Ionotropic glutamate receptorsCrystal structureExcitatory neurotransmissionAssemblyGlutamate receptorsPropose mechanismsReceptorsSubunitsDomainProteinAssemblagesNMDA receptors
2005
Subunit arrangement and function in NMDA receptors
Furukawa H, Singh SK, Mancusso R, Gouaux E. Subunit arrangement and function in NMDA receptors. Nature 2005, 438: 185-192. PMID: 16281028, DOI: 10.1038/nature04089.Peer-Reviewed Original ResearchConceptsHeteromeric ion channelsNR1-NR2AMammalian central nervous systemSlow channel openingChannel openingHeterodimer interfaceTransduction cascadeIon channel openingSubunit arrangementSubunit interfaceIon channelsNR2 subunitsReceptor functionChannel deactivationNMDA receptorsNMDA receptor functionReceptorsExcitatory neurotransmissionFunctional unitsCentral nervous systemNR1GlutamateGlycineNervous systemHeterodimers