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
Site-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