Search results for "units"

showing 10 items of 576 documents

Pharmacological activity of C10-substituted analogs of the high-affinity kainate receptor agonist dysiherbaine

2009

Kainate receptor antagonists have potential as therapeutic agents in a number of neuropathologies. Synthetic modification of the convulsant marine toxin neodysiherbaine A (NDH) previously yielded molecules with a diverse set of pharmacological actions on kainate receptors. Here we characterize three new synthetic analogs of NDH that contain substituents at the C10 position in the pyran ring of the marine toxin. The analogs exhibited high-affinity binding to the GluK1 (GluR5) subunit and lower affinity binding to GluK2 (GluR6) and GluK3 (GluR7) subunits in radioligand displacement assays with recombinant kainate and AMPA receptors. As well, the natural toxin NDH exhibited approximately 100-f…

Models MolecularAgonistKainic acidPatch-Clamp TechniquesTime FactorsStereochemistrymedicine.drug_classProtein subunitGreen Fluorescent ProteinsGlutamic AcidKainate receptorAMPA receptorMolecular Dynamics SimulationLigandsTransfectionTritiumBinding CompetitiveArticleMembrane PotentialsRadioligand AssayStructure-Activity RelationshipCellular and Molecular Neurosciencechemistry.chemical_compoundReceptors Kainic AcidExcitatory Amino Acid AgonistsmedicineRadioligandHumansReceptoralpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic AcidCell Line TransformedPharmacologyAlanineKainic AcidDose-Response Relationship DrugMolecular StructureChemistryBridged Bicyclo Compounds HeterocyclicProtein SubunitsBiochemistryMutagenesis Site-DirectedMarine toxinNeuropharmacology
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Full Domain Closure of the Ligand-binding Core of the Ionotropic Glutamate Receptor iGluR5 Induced by the High Affinity Agonist Dysiherbaine and the …

2009

The prevailing structural model for ligand activation of ionotropic glutamate receptors posits that agonist efficacy arises from the stability and magnitude of induced domain closure in the ligand-binding core structure. Here we describe an exception to the correlation between ligand efficacy and domain closure. A weakly efficacious partial agonist of very low potency for homomeric iGluR5 kainate receptors, 8,9-dideoxyneodysiherbaine (MSVIII-19), induced a fully closed iGluR5 ligand-binding core. The degree of relative domain closure, approximately 30 degrees , was similar to that we resolved with the structurally related high affinity agonist dysiherbaine and to that of l-glutamate. The ph…

Models MolecularAgonistStereochemistrymedicine.drug_classGlutamic AcidKainate receptorCrystallography X-RayLigandsBiochemistryPartial agonistCell LineReceptors Kainic AcidmedicineHumansComputer SimulationAmino AcidsReceptorMolecular BiologyAlanineBinding SitesChemistryMechanisms of Signal TransductionGlutamate receptorHydrogen BondingCell BiologyBridged Bicyclo Compounds HeterocyclicLigand (biochemistry)Protein Structure TertiaryProtein SubunitsIonotropic glutamate receptorProtein BindingIonotropic effectJournal of Biological Chemistry
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Functional cysteine-less subunits of the transporter associated with antigen processing (TAP1 and TAP2) by de novo gene assembly

2002

AbstractWithin the adaptive immune system the transporter associated with antigen processing (TAP) plays a pivotal role in loading of peptides onto major histocompatibility (MHC) class I molecules. As a central tool to investigate the structure and function of the TAP complex, we created cysteine-less human TAP subunits by de novo gene synthesis, replacing all 19 cysteines in TAP1 and TAP2. After expression in TAP-deficient human fibroblasts, cysteine-less TAP1 and TAP2 are functional with respect to adenosine triphosphate (ATP)-dependent peptide transport and inhibition by ICP47 from herpes simplex virus. Cysteine-less TAP1 and TAP2 restore maturation and intracellular trafficking of MHC c…

Models MolecularBiophysicsBiological Transport ActiveBiologyMajor histocompatibility complexTransfectionBiochemistryCell Linechemistry.chemical_compoundAdenosine TriphosphateStructural BiologyATP Binding Cassette Transporter Subfamily B Member 3Cysteine-scanning mutagenesisMHC class IGeneticsHumansCysteineATP Binding Cassette Transporter Subfamily B Member 2Molecular BiologyAntigen PresentationAntigen processingHistocompatibility Antigens Class ICell BiologyTransporter associated with antigen processingMolecular biologyRecombinant ProteinsCell biologyProtein SubunitschemistryAmino Acid SubstitutionAntigen processingPeptide transportMembrane proteinbiology.proteinAdenosine triphosphate-binding cassette transporterTAP2ATP-Binding Cassette TransportersTAP1Adenosine triphosphateFEBS Letters
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Introduction of histidine residues into avidin subunit interfaces allows pH-dependent regulation of quaternary structure and biotin binding

2003

AbstractIn order to turn the subunit association and biotin binding of avidin into pH-sensitive phenomena, we have replaced individually three amino acid residues in avidin (Met96, Val115 and Ile117) with histidines in the 1–3 interface, and in combination with a histidine conversion in the 1–2 interface (Trp110). The single replacements Met96His and Val115His in the 1–3 interface were found to have a clear effect on the quaternary structure of avidin, since subunit associations of these mutants became pH-dependent. The histidine replacement in the 1–2 interface affected the biotin-binding properties of the mutants, in particular reversibility of binding and protein–ligand complex formation…

Models MolecularBiotin bindingInsectaProtein subunitBiophysicsBiotinBiosensing TechniquesBiochemistryCell LineProtein structureStructural BiologyGeneticsAnimalsHistidinepH dependenceProtein Structure QuaternaryMolecular BiologyHistidinebiologyChemistryCell BiologyProtein engineeringHydrogen-Ion ConcentrationAvidinRecombinant ProteinsMolecular WeightProtein SubunitsSpectrometry FluorescenceAmino Acid SubstitutionBiochemistryBiotinylationBiophysicsbiology.proteinProtein quaternary structureProtein engineeringBaculoviridaeProtein BindingAvidinFEBS Letters
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Tetravalent single-chain avidin: from subunits to protein domains via circularly permuted avidins

2005

scAvd (single-chain avidin, where two dcAvd are joined in a single polypeptide chain), having four biotin-binding domains, was constructed by fusion of topologically modified avidin units. scAvd showed similar biotin binding and thermal stability properties as chicken avidin. The DNA construct encoding scAvd contains four circularly permuted avidin domains, plus short linkers connecting the four domains into a single polypeptide chain. In contrast with wild-type avidin, which contains four identical avidin monomers, scAvd enables each one of the four avidin domains to be independently modified by protein engineering. Therefore the scAvd scaffold can be used to construct spatially and stoich…

Models MolecularBiotin bindingProtein domainMolecular Sequence DataProtein EngineeringBiochemistrychemistry.chemical_compoundMoleculeAnimalsMolecular BiologyCells CulturedBinding SitesbiologyChemistryCell BiologyProtein engineeringCircular permutation in proteinsAvidinProtein Structure TertiaryCrystallographyProtein SubunitsMonomerBiophysicsbiology.proteinDNA constructChickensAvidinResearch ArticleProtein Binding
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Insights into the catalytic mechanism of human sEH phosphatase by site-directed mutagenesis and LC-MS/MS analysis

2008

We have recently reported that human soluble epoxide hydrolase (sEH) is a bifunctional enzyme with a novel phosphatase enzymatic activity. Based on a structural relationship with other members of the haloacid dehalogenase superfamily, the sEH N-terminal phosphatase domain revealed four conserved sequence motifs, including the proposed catalytic nucleophile D9, and several other residues potentially implicated in substrate turnover and/or Mg(2+) binding. To enlighten the catalytic mechanism of dephosphorylation, we constructed sEH phosphatase active-site mutants by site-directed mutagenesis. A total of 18 mutants were constructed and recombinantly expressed in Escherichia coli as soluble pro…

Models MolecularEpoxide hydrolase 2Molecular Sequence DataPhosphatase10050 Institute of Pharmacology and Toxicology610 Medicine & healthMass SpectrometryPhosphatesDephosphorylation1315 Structural BiologyProtein structureStructural Biology1312 Molecular BiologyHumansPhosphofructokinase 2Amino Acid SequenceBinding siteProtein Structure QuaternarySite-directed mutagenesisMolecular BiologyEpoxide HydrolasesBinding SitesChemistrySubstrate (chemistry)Phosphoric Monoester HydrolasesRecombinant ProteinsProtein Structure TertiaryProtein SubunitsBiochemistryMutagenesis Site-Directed570 Life sciences; biologyDimerizationSequence AlignmentChromatography Liquid
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Structural Mechanism of SDS-Induced Enzyme Activity of Scorpion Hemocyanin Revealed by Electron Cryomicroscopy

2009

Summary Phenoloxidases (POs) occur in all organisms and are involved in skin and hair coloring in mammals, and initiating melanization in wound healing. Mutation or overexpression of PO can cause albinism or melanoma, respectively. SDS can convert inactive PO and the oxygen carrier hemocyanin (Hc) into enzymatically active PO. Here we present single-particle cryo-EM maps at subnanometer resolution and pseudoatomic models of the 24-oligomeric Hc from scorpion Pandinus imperator in resting and SDS-activated states. Our structural analyses led to a plausible mechanism of Hc enzyme PO activation: upon SDS activation, the intrinsically flexible Hc domain I twists away from domains II and III in …

Models MolecularPROTEINSCopper proteinProtein Conformationmedicine.medical_treatmentProtein subunitArticleScorpions03 medical and health sciencesEnzyme activatorSurface-Active AgentsProtein structureStructural BiologyCatalytic DomainmedicineAnimalsBinding siteMolecular Biology030304 developmental biology0303 health sciencesBinding SitesbiologyChemistryMonophenol Monooxygenase030302 biochemistry & molecular biologyCryoelectron MicroscopyActive siteSodium Dodecyl SulfateHemocyaninEnzyme ActivationProtein SubunitsBiochemistryHemocyaninsbiology.proteinOxygen bindingStructure
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Quaternary structure of the European spiny lobster (Palinurus elephas) 1x6-mer hemocyanin from cryoEM and amino acid sequence data.

2002

Abstract Arthropod hemocyanins are large respiratory proteins that are composed of up to 48 subunits (8×6-mer) in the 75 kDa range. A 3D reconstruction of the 1×6-mer hemocyanin from the European spiny lobster Palinurus elephas has been performed from 9970 single particles using cryoelectron microscopy. An 8 A resolution of the hemocyanin 3D reconstruction has been obtained from about 600 final class averages. Visualisation of structural elements such as α-helices has been achieved. An amino acid sequence alignment shows the high sequence identity (>80%) of the hemocyanin subunits from the European spiny lobster P. elephas and the American spiny lobster Panulirus interruptus . Comparison of…

Models MolecularPanulirusmedicine.medical_treatmentPalinurus elephasMolecular Sequence DataStatic ElectricityCrystallography X-RaySpecies SpecificityStructural BiologymedicineAnimalsAmino Acid SequencePalinuridaeProtein Structure QuaternaryMolecular BiologyPeptide sequencebiologySequence Homology Amino AcidResolution (electron density)Cryoelectron MicroscopyHemocyaninbiology.organism_classificationCrystallographyProtein SubunitsBiochemistryHemocyaninsProtein quaternary structureArthropodSpiny lobsterSequence AlignmentJournal of molecular biology
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Synthesis of GABAA receptor agonists and evaluation of their alpha-subunit selectivity and orientation in the GABA binding site.

2008

Drugs used to treat various disorders target GABA A receptors. To develop alpha subunit selective compounds, we synthesized 5-(4-piperidyl)-3-isoxazolol (4-PIOL) derivatives. The 3-isoxazolol moiety was substituted by 1,3,5-oxadiazol-2-one, 1,3,5-oxadiazol-2-thione, and substituted 1,2,4-triazol-3-ol heterocycles with modifications to the basic piperidine substituent as well as substituents without basic nitrogen. Compounds were screened by [(3)H]muscimol binding and in patch-clamp experiments with heterologously expressed GABA A alpha ibeta 3gamma 2 receptors (i = 1-6). The effects of 5-aminomethyl-3 H-[1,3,4]oxadiazol-2-one 5d were comparable to GABA for all alpha subunit isoforms. 5-pipe…

Models MolecularPatch-Clamp TechniquesStereochemistryAlpha (ethology)gamma-Aminobutyric acidArticleGABAA-rho receptorCell Linechemistry.chemical_compoundStructure-Activity RelationshipXenopus laevisPiperidinesDrug DiscoverymedicineAnimalsHumansGABA-A Receptor AgonistsBinding siteReceptorgamma-Aminobutyric AcidG alpha subunitBinding SitesMolecular StructureChemistryGABAA receptorMuscimolBrainIsoxazolesReceptors GABA-ARatsElectrophysiologyProtein SubunitsBiochemistryMuscimolMutationOocytesMolecular MedicineFemalemedicine.drugJournal of medicinal chemistry
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Ligand-binding domain determines endoplasmic reticulum exit of AMPA receptors.

2010

AMPA receptors (AMPARs) are tetrameric ion channels that mediate rapid glutamate signaling in neurons and many non-neuronal cell types. Endoplasmic reticulum (ER) quality control mechanisms permit only correctly folded functional receptors to be delivered to the cell surface. We analyzed the biosynthetic maturation and transport of all 12 GluA1–4 subunit splice variants as homomeric receptors and observed robust isoform-dependent differences in ER exit competence and surface expression. In contrast to inefficient ER exit of both GluA3 splice forms and the flop variants of GluA1 and GluA4, prominent plasma membrane expression was observed for the other AMPAR isoforms. Surprisingly, deletion …

Models MolecularProtein ConformationImmunoblottingMolecular Sequence DataAMPA receptorBiologymedicine.disease_causeEndoplasmic ReticulumLigandsBiochemistryCell membrane03 medical and health sciences0302 clinical medicineNeurobiologyProtein targetingChlorocebus aethiopsmedicineHomomericAnimalsHumansProtein IsoformsAmino Acid SequenceReceptors AMPAReceptorMolecular BiologyIon channel030304 developmental biology0303 health sciencesBinding SitesSequence Homology Amino AcidEndoplasmic reticulumCell MembraneCell BiologyCell biologyTransport proteinProtein Structure TertiaryAlternative SplicingProtein SubunitsProtein Transportmedicine.anatomical_structureHEK293 CellsMicroscopy FluorescenceCOS CellsProtein Multimerization030217 neurology & neurosurgeryThe Journal of biological chemistry
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