2016
The Pharmacochaperone Activity of Quinine on Bitter Taste Receptors
Upadhyaya J, Chakraborty R, Shaik F, Jaggupilli A, Bhullar R, Chelikani P. The Pharmacochaperone Activity of Quinine on Bitter Taste Receptors. PLOS ONE 2016, 11: e0156347. PMID: 27223611, PMCID: PMC4880206, DOI: 10.1371/journal.pone.0156347.Peer-Reviewed Original ResearchConceptsBitter taste receptorsBitter taste signal transductionTaste receptorsTaste signal transductionControl untreated cellsQuinine treatmentAgonist treatmentCell surface expressionCalcium responsePharmacological techniquesAgonist activityTaste sensationBitter agonistsBasic taste sensationsReceptor internalizationSurface expressionUntreated cellsQuinineTreatmentDesensitizationReceptorsSignal transductionObserved actions
2013
New Insights into Structural Determinants for Prostanoid Thromboxane A2 Receptor- and Prostacyclin Receptor-G Protein Coupling
Chakraborty R, Pydi SP, Gleim S, Bhullar RP, Hwa J, Dakshinamurti S, Chelikani P. New Insights into Structural Determinants for Prostanoid Thromboxane A2 Receptor- and Prostacyclin Receptor-G Protein Coupling. Molecular And Cellular Biology 2013, 33: 184-193. PMID: 23109431, PMCID: PMC3554117, DOI: 10.1128/mcb.00725-12.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesCalciumFluorescent Antibody TechniqueGTP-Binding ProteinsHEK293 CellsHumansInositol 1,4,5-TrisphosphateLigandsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedNonlinear DynamicsProtein BindingProtein ConformationReceptors, EpoprostenolReceptors, Thromboxane A2, Prostaglandin H2Signal TransductionConceptsG protein-coupled receptorsG protein specificityThromboxane A2 receptorProtein interactionsProtein specificityIntracellular loopChimeric receptorsG proteinsGPCR-G protein interactionsProtein couplingHeterotrimeric G proteinsCognate G-proteinSite-directed mutagenesisNew molecular insightsProtein-coupled receptorsG protein couplingReceptor-G protein interactionG protein activationA2 receptorsReceptor-G protein couplingStructural basisMolecular insightsProtein activationMolecular natureStructural determinants
2012
Role of rhodopsin N-terminus in structure and function of rhodopsin-bitter taste receptor chimeras
Pydi S, Chakraborty R, Bhullar R, Chelikani P. Role of rhodopsin N-terminus in structure and function of rhodopsin-bitter taste receptor chimeras. Biochemical And Biophysical Research Communications 2012, 430: 179-182. PMID: 23159609, DOI: 10.1016/j.bbrc.2012.11.029.Peer-Reviewed Original ResearchConceptsG protein-coupled receptorsBitter taste receptorsTaste receptorsProtein-coupled receptorsBitter taste sensationReceptor expressionLow-level expressionCalcium imagingReceptor functionFlow cytometryReceptorsTaste sensationAllosteric ligand bindingT2RsReceptor chimerasAmino acidsExpressionReceptor structureN-terminal 33N-terminal 33 amino acidsN-terminal sequenceCytometrySite-Directed Mutations and the Polymorphic Variant Ala160Thr in the Human Thromboxane Receptor Uncover a Structural Role for Transmembrane Helix 4
Chakraborty R, Pydi SP, Gleim S, Dakshinamurti S, Hwa J, Chelikani P. Site-Directed Mutations and the Polymorphic Variant Ala160Thr in the Human Thromboxane Receptor Uncover a Structural Role for Transmembrane Helix 4. PLOS ONE 2012, 7: e29996. PMID: 22272267, PMCID: PMC3260207, DOI: 10.1371/journal.pone.0029996.Peer-Reviewed Original ResearchMeSH Keywords15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic AcidAlanineAmino Acid SequenceAnimalsBinding SitesBinding, CompetitiveBridged Bicyclo Compounds, HeterocyclicCalciumChlorocebus aethiopsCOS CellsFatty Acids, UnsaturatedGlycineHEK293 CellsHumansHydrazinesMicroscopy, FluorescenceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutant ProteinsMutation, MissensePolymorphism, Single NucleotideProtein Structure, SecondaryRadioligand AssayReceptors, Thromboxane A2, Prostaglandin H2Structure-Activity RelationshipTemperature
2011
Structural and functional roles of small group-conserved amino acids present on helix-H7 in the β2-adrenergic receptor
Arakawa M, Chakraborty R, Upadhyaya J, Eilers M, Reeves P, Smith S, Chelikani P. Structural and functional roles of small group-conserved amino acids present on helix-H7 in the β2-adrenergic receptor. Biochimica Et Biophysica Acta 2011, 1808: 1170-1178. PMID: 21262196, PMCID: PMC3062665, DOI: 10.1016/j.bbamem.2011.01.012.Peer-Reviewed Original ResearchAdrenergic beta-AgonistsAdrenergic beta-AntagonistsAmino Acid SubstitutionAmino AcidsAnimalsBinding SitesChlorocebus aethiopsCOS CellsCricetinaeCyclic AMPDihydroalprenololGlycineHEK293 CellsHumansHydrogen BondingIsoproterenolModels, MolecularMutationProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryRadioligand AssayReceptors, Adrenergic, beta-2SerineStructure-Activity Relationship