Search results for "binding site"

showing 10 items of 856 documents

Cooperative Transition in the Conformation of 24-Mer Tarantula Hemocyanin upon Oxygen Binding

2005

Hemocyanins are large respiratory proteins of arthropods and mollusks, which bind oxygen with very high cooperativity. Here, we investigated the relationship between oxygen binding and structural changes of the 24-mer tarantula hemocyanin. Oxygen binding of the hemocyanin was detected following the fluorescence intensity of the intrinsic tryptophans. Under the same conditions, structural changes were monitored by the non-covalently bound fluorescence probe Prodan (6-propionyl-2-(dimethylamino)-naphthalene), which is very sensitive to its surroundings. Upon oxygen binding of the hemocyanin a red shift of 5 nm in the emission maximum of the label was observed. A comparison of oxygen binding c…

Macromolecular SubstancesProtein ConformationPartial Pressuremedicine.medical_treatmentAllosteric regulationMolecular ConformationAnalytical chemistrychemistry.chemical_elementchemical and pharmacologic phenomenaCooperativitycomplex mixturesBiochemistryOxygenProtein structure2-NaphthylaminemedicineAnimalsBinding siteMolecular BiologyBinding SitesChemistryTryptophanSpidersHemocyaninCell BiologyFluorescenceOxygenSpectrometry FluorescenceMicroscopy FluorescenceModels ChemicalSpectrophotometryHemocyaninsBiophysicsAllosteric SiteOxygen bindingProtein BindingJournal of Biological Chemistry
researchProduct

Transient structural ordering of the RNA-binding domain of carnation mottle virus p7 movement protein modulates nucleic acid binding.

2005

Plant viral movement proteins bind to RNA and participate in the intra- and intercellular movement of the RNAs from plant viruses. However, the role and magnitude of the conformational changes associated with the formation of RNA-protein complexes are not yet defined. Here we describe studies on the relevance of a preexisting nascent alpha-helix at the C terminus of the RNA-binding domain of p7, a movement protein from carnation mottle virus, to RNA binding. Synthetic peptide analogues and single amino acid mutation at the RNA-binding domain of recombinant p7 protein were used to correlate the transient structural order in aqueous solution with RNA-binding potential.

Magnetic Resonance SpectroscopyMolecular Sequence DataBiochemistryViral ProteinsPlant virusAmino Acid SequenceBinding siteMovement proteinMolecular BiologyBinding SitesbiologyC-terminusOrganic ChemistryRNARNA-Binding Proteinsbiology.organism_classificationRecombinant ProteinsProtein Structure TertiarySpectrometry FluorescenceBiochemistryCarnation mottle virusMutationNucleic acidMolecular MedicineRNAPeptidesBinding domainChembiochem : a European journal of chemical biology
researchProduct

Paramagnetic Cobalt and Nickel Derivatives of Alcaligenes denitrificans Azurin and Its M121Q Mutant. A 1H NMR Study

1996

Using cobalt or nickel to replace copper in native azurin allows one to fingerprint the metal coordination site of the protein. The metal sites of wild type Alcaligenes denitrificans azurin and its M121Q mutant are clearly distinguishable through the paramagnetic 1H NMR spectra of the Ni(II) and Co(II) derivatives. In the wild type azurin, Gly45 coordinates to nickel or cobalt, while Met121 appears as a weak metal ligand. On the contrary, in the M121Q azurin mutant, the metal exhibits a clear preference for the Gln121, which coordinates through the side chain carbonyl oxygen, and Gly45 is not a ligand. Changes in the isotropic shifts and relaxation properties of signals from the Cys112, His…

Magnetic Resonance SpectroscopyProtein ConformationStereochemistryAlcaligenes denitrificanschemistry.chemical_elementBiochemistryElectron TransportMetalAzurinNickelMetalloproteinsPoint MutationAlcaligenesPlant ProteinsBinding SitesStellacyaninMolecular StructurebiologyLigandCobaltbiology.organism_classificationNMR spectra databaseNickelchemistrySpectrophotometryvisual_artvisual_art.visual_art_mediumbiology.proteinSpectrophotometry UltravioletAzurinCobaltBiochemistry
researchProduct

An NMR Study of the Interaction of 15N-Labelled Bradykinin with an Antibody Mimic of the Bradykinin B2 Receptor

1997

An isotope-edited NMR study of the peptide hormone bradykinin (RPPGFSPFR) bound to the Fab fragment of a monoclonal antibody against bradykinin (MBK3) is reported. MBK3 was previously shown to provide a binding site model of the B2 bradykinin receptor [Haasemann, M., Buschko, J., Faussner, A., Roscher, A. A., Hoebeke, J., Burch, R. M. & Muller-Esterl, W. (1991) Anti-idiotypic antibodies bearing the internal image of a bradykinin epitope, J. Immunol. 147, 3882-3892]. Bradykinin was obtained in a uniformly 15N-labelled form using recombinant expression of a fusion protein consisting of the glutathione-binding domain of glutathione S-transferase fused to residues 354-375 of the high-molecular-…

Magnetic Resonance SpectroscopyReceptor Bradykinin B2Protein ConformationStereochemistryRecombinant Fusion ProteinsBradykininIn Vitro TechniquesBradykininBiochemistryImmunoglobulin Fab FragmentsMicechemistry.chemical_compoundAnimalsHumansAmino Acid SequenceBradykinin receptorDNA PrimersKininogenBinding SitesBase SequenceNitrogen IsotopesChemistryReceptors BradykininImmunoglobulin Fab FragmentsProteolytic enzymesAntibodies MonoclonalNuclear magnetic resonance spectroscopyB2 Bradykinin ReceptorTwo-dimensional nuclear magnetic resonance spectroscopyProtein BindingEuropean Journal of Biochemistry
researchProduct

Organotypic rat cerebellar slice culture as a model to analyze the molecular pharmacology of GABAA receptors

2002

The preservation of the neuronal circuitry in rat cerebellar slice cultures provides an advantage in monitoring the development and characterizing the pharmacology of GABA(A) receptor subtypes. Sprague-Dawley rats, 8-11 days of age, were decapitated, their cerebella were cut into 400-microm slices and transferred into culture dishes. Cell viability and organotypic cerebellar organization of the culture remained well preserved up to 3 weeks. Autoradiographic procedures were introduced in these advanced culture technique and employed [(3)H]Ro 15-4513 in the absence and presence of 10 microM diazepam to visualize all benzodiazepine (BZD) and diazepam-insensitive (DIS) binding sites, respective…

MaleAgonistAzidesCerebellumCell Survivalmedicine.drug_classProtein subunitBiologyPharmacologyRats Sprague-DawleyBenzodiazepinesCerebellumCulture TechniquesmedicineAnimalsPharmacology (medical)Viability assayReceptorCells CulturedBiological PsychiatryPharmacologyBenzodiazepineBinding SitesGABAA receptorAffinity LabelsReceptors GABA-ARatsPsychiatry and Mental healthmedicine.anatomical_structureAnimals NewbornNeurologyOrgan SpecificityNeurology (clinical)NeuroscienceDiazepammedicine.drugEuropean Neuropsychopharmacology
researchProduct

Characterization of γ-aminobutyrate type A receptors with atypical coupling between agonist and convulsant binding sites in discrete brain regions

2001

Abstract γ-Aminobutyric acid type A (GABA A ) receptor ionophore ligand t -[ 35 S]butylbicyclophosphorothionate ([ 35 S]TBPS) was used in an autoradiographic assay on brain cryostat sections to visualize and characterize atypical GABA-insensitive [ 35 S]TBPS binding previously described in certain recombinant GABA A receptors and the cerebellar granule cell layer. Picrotoxinin-sensitive but 1-mM GABA-insensitive [ 35 S]TBPS binding was present in the rat cerebellar granule cell layer, many thalamic nuclei, subiculum and the internal rim of the cerebral cortex, amounting in these regions up to 6% of the basal binding determined in the absence of exogenous GABA. Similar binding properties wer…

MaleAgonistAzidesmedicine.medical_specialtyCerebellumSesterterpenesmedicine.drug_classLoreclezoleConvulsantsBiologySulfur RadioisotopesTritiumBinding CompetitiveBenzodiazepinesRadioligand AssayCellular and Molecular Neurosciencechemistry.chemical_compoundThalamusCerebellumInternal medicinemedicineAnimalsHumansPicrotoxinRats WistarBinding siteReceptorGABA AgonistsMolecular Biologygamma-Aminobutyric AcidMuscimolGABAA receptorAffinity LabelsBridged Bicyclo Compounds HeterocyclicReceptors GABA-AGranule cellRatsEndocrinologymedicine.anatomical_structurenervous systemMuscimolchemistryBiophysicsChickensmedicine.drugMolecular Brain Research
researchProduct

The effects of several muscarinic antagonists on pre- and postsynaptic receptors in the isolated rabbit heart

1981

In order to reveal possible differences between pre- and postsynaptic muscarine receptors, seven antagonists were tested for their affinities on these receptor sites in the rabbit isolated perfused heart. Methacholine was used as an agonist to inhibit the noradrenaline overflow evoked by electrical stimulation (3 Hz, 3 min) of the sympathetic nerves (presynaptic parameter) and to decrease the systolic tension development of the right atrium (postsynaptic parameter). The affinity of an antagonist was expressed as pA2. A decreasing order of potency was obtained with ipratropium, scopolamine, atropine, trihexyphenidyl, amitriptyline, and gallamine, both for pre- and postsynaptic responses. The…

MaleAgonistmedicine.medical_specialtymedicine.drug_classPopulationStimulationIn Vitro TechniquesNorepinephrinechemistry.chemical_compoundPostsynaptic potentialInternal medicineMuscarinic acetylcholine receptormedicineAnimalsMethacholine CompoundsReceptors CholinergicReceptoreducationPharmacologyeducation.field_of_studyBinding SitesMuscarineDose-Response Relationship DrugGallamine TriethiodideMyocardiumParasympatholyticsGeneral MedicineReceptors MuscarinicReceptors NeurotransmitterEndocrinologychemistryFemaleMethacholineRabbitsmedicine.drugNaunyn-Schmiedeberg's Archives of Pharmacology
researchProduct

Altered receptor subtypes in the forebrain of GABAA receptor δ subunit-deficient mice: recruitment of γ2 subunits

2002

A GABA(A) receptor delta subunit-deficient mouse line was created by homologous recombination in embryonic stem cells to investigate the role of the subunit in the brain GABA(A) receptors. High-affinity [(3)H]muscimol binding to GABA sites as studied by ligand autoradiography was reduced in various brain regions of delta(-/-) animals. [(3)H]Ro 15-4513 binding to benzodiazepine sites was increased in delta(-/-) animals, partly due to an increment of diazepam-insensitive receptors, indicating an augmented forebrain assembly of gamma 2 subunits with alpha 4 subunits. In the western blots of forebrain membranes of delta(-/-) animals, the level of gamma 2 subunit was increased and that of alpha …

MaleAzidesProtein subunitBiologyTritiumSynaptic TransmissionIon ChannelsGABAA-rho receptorInterleukin 10 receptor alpha subunitBenzodiazepinesMiceRadioligand Assaychemistry.chemical_compoundAnimalsReceptorGABA Agonistsgamma-Aminobutyric AcidMice KnockoutNeuronsBinding SitesMuscimolGABAA receptorGeneral NeuroscienceBrainAffinity LabelsNeural InhibitionReceptors GABA-AMolecular biologynervous systemMuscimolchemistryMutationForebrainFemaleCys-loop receptorsNeuroscience
researchProduct

Interaction of uridine with GABA binding sites in cerebellar membranes of the rat

1983

The effect of uridine, a postulated anticonvulsant agent, on GABA receptors has been investigated. Uridine inhibits [3H]GABA binding to rat cerebellar buffer-washed membranes. Pretreatment of the membranes with Triton X-100 increases the effect of uridine on GABA-binding. The Scatchard analysis reveals that both high and low affinities of GABA for its receptors are affected by 1 mM uridine, while the apparent number of binding sites remains unchanged. The ability of uridine to interact competitively with GABA binding sites, also examined by the Lineweaver-Burk analysis, suggests a possible mechanism of action of this anticonvulsant agent, so including it among those compounds characterized …

MaleCerebellumReceptors Cell SurfaceBiologyBinding CompetitiveBiochemistrygamma-Aminobutyric acidCellular and Molecular Neurosciencechemistry.chemical_compoundGABA receptorCerebellummedicineAnimalsBinding siteReceptorUridinegamma-Aminobutyric AcidGABAA receptorCell MembraneRats Inbred StrainsGeneral MedicineReceptors GABA-AUridineRatsmedicine.anatomical_structurenervous systemBiochemistryMechanism of actionchemistryAnticonvulsantsmedicine.symptommedicine.drugNeurochemical Research
researchProduct

Lateral differences in GABA binding sites in rat brain.

1988

An asymmetric distribution of GABA binding sites was found in the cerebral cortex, hippocampus, cerebellar hemispheres, striatum, and thalamus. Higher levels of [3H]GABA binding were observed in the left-side of most brain areas and in a greater percentage of adult rats, but the opposite asymmetry was found in the thalamus. A similar left-right difference in cerebral hemispheres was also found in five day-old rats, suggesting the genetic predetermination of asymmetry.

MaleCerebellumThalamusCentral nervous systemHippocampusStriatumBiochemistryHippocampusFunctional LateralityCellular and Molecular NeurosciencemedicineAnimalsBinding siteCerebral CortexBinding SitesChemistryBrainRats Inbred StrainsGeneral MedicineReceptors GABA-AhumanitiesCorpus StriatumRatsmedicine.anatomical_structurenervous systemCerebral cortexCerebral hemisphereNeuroscienceNeurochemical research
researchProduct