Search results for "binding site"

showing 10 items of 856 documents

Characterization of a common binding site for basic drugs on human ?2-acid glycoprotein (orosomucoid)

1983

The interaction of chlorpromazine, dl-propranolol, and imipramine with isolated α1-acid glycoprotein is characterized by relatively high association constants and only one binding site per protein molecule. The mutual displacement between the three drugs indicates that all three compounds are bound to the same binding site. Several other basic drugs from different pharmacological and chemical classes also displace chlorpromazine, dl-propranolol, and imipramine with potencies, one would predict from their association constants or from the degree of their plasma binding in humans. It is concluded that displacement phenomena like those observed in this study in vitro are likely to occur also i…

Pharmacologychemistry.chemical_classificationbiologyChemistryOrosomucoidGeneral MedicineImipramineIn vitroBiochemistryIn vivomedicinebiology.proteinMoleculeBinding siteGlycoproteinChlorpromazinemedicine.drugNaunyn-Schmiedeberg's Archives of Pharmacology
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8-NH2-Boldine, an Antagonist of α1Aand α1BAdrenoceptors without Affinity for the α1DSubtype: Structural Requirements for Aporphines at α1-Adrenocepto…

2005

Structure-activity analysis of 21 aporphine derivatives was performed by examining their affinities for cloned human alpha (1A), alpha (1B) and alpha (1D) adrenoceptors (AR) using membranes prepared from rat-1 fibroblasts stably expressing each alpha (1)-AR subtype. All the compounds tested competed for [ (125)I]-HEAT binding with steep and monophasic curves. The most interesting compound was 8-NH (2)-boldine, which retains the selective affinity for alpha(1A)-AR (pKi = 6.37 +/- 0.21) vs. alpha(1B)-AR (pKi = 5.53 +/- 0.11) exhibited by 1,2,9,10-tetraoxygenated aporphines, but shows low affinity for alpha(1D)-AR (pKi < 2.5). Binding studies on native adrenoceptors present in rat cerebral cor…

Pharmacologychemistry.chemical_classificationeducation.field_of_studyAdrenergic receptorStereochemistryOrganic ChemistryPopulationAntagonistPharmaceutical ScienceBiologyAnalytical Chemistrychemistry.chemical_compoundComplementary and alternative medicinechemistryDrug DiscoveryMolecular MedicineStructure–activity relationshipBoldineAporphineBinding siteInositol phosphateeducationPlanta Medica
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Relationships between structure and vascular activity in a series of benzylisoquinolines

1997

1 1In the present work, the properties of 3-methyl isoquinoline, 3,4-dihydropapaverine, tetrahydropapaverine and tetrahydropapaveroline were compared with those of papaverine and laudanosine. The work includes functional studies on rat isolated aorta contracted with noradrenaline, caffeine or KC1, and a determination of the affinity of the compounds for α1-adrenoceptors and calcium channel binding sites, with [#H]-prazosin, [#H]-nitrendipine and [#H]-(+)-cis-diltiazem binding to rat cerebral cortical membranes. The effects of papaverine derivatives on the different molecular forms of cyclic nucleotide phosphodiesterases (PDE) isolated from bovine aorta were also determined. 2 2The three pap…

Pharmacologymedicine.medical_specialtyPapaverineTetrahydroisoquinolineAlkaloidPhosphodiesterasePharmacologyLaudanosinechemistry.chemical_compoundEndocrinologychemistryMechanism of actionInternal medicinemedicineIsoquinolineBinding sitemedicine.symptommedicine.drugBritish Journal of Pharmacology
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Hydrolytic action of phospholipase A2 in monolayers in the phase transition region: direct observation of enzyme domain formation using fluorescence …

1990

Phospholipase A2, a ubiquitous lipolytic enzyme highly active in the hydrolysis of organized phospholipid substrates, has been characterized optically in its action against a variety of phospholipid monolayers using fluorescence microscopy. By labeling the enzyme with a fluorescent marker and introducing it into the subphase of a Langmuir film balance, the hydrolysis of lipid monolayers in their liquid-solid phase transition region could be directly observed with the assistance of an epifluorescence microscope. Visual observation of hydrolysis of different phospholipid monolayers in the phase transition region in real-time could differentiate various mechanisms of hydrolytic action against …

Phase transition12-DipalmitoylphosphatidylcholineStereochemistryBiophysicsPhospholipidBiochemistryPhospholipases Achemistry.chemical_compoundPhospholipase A2Phase (matter)MonolayerEnzyme StabilityFluorescence microscopeLipid bilayer phase behaviorParticle SizePhospholipidsFluorescent DyesElapid VenomsPhospholipase ABinding SitesbiologyHydrolysisPhosphatidylethanolaminesCell BiologyImage EnhancementPhospholipases A2chemistryMicroscopy FluorescencePhospholipasesBiophysicsbiology.proteinlipids (amino acids peptides and proteins)DimyristoylphosphatidylcholineBiochimica et biophysica acta
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PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163

1996

AbstractThe 80kDa Myristolated Alanine-Rich C-Kinase Substrate (MARCKS) in a major in vivo substrate of protein kinase C (PKC). Here we report that MARCKS is a major substrate for the lipid-activated PKC-related kinase (PRK1) in cell extracts. Furthermore, PRK1 is shown to phosphorylate MARCKS on the same sites as PKC in vitro. Thus, control of MARCKS phosphorylation on these previously identified ‘PKC’ sites may be regulated under certain circumstances by PRK as well as PKC mediated signalling pathways. The implications for MARCKS as a marker of PKC activation and as a point of signal convergence are discussed.

PhosphopeptidesMARCKSPRKRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsKidneyBiochemistryCell-free systemCell LineSerineStructural BiologyProtein kinase CGeneticsAnimalsAmino Acid SequenceBinding siteMARCKSPKCPhosphorylationMyristoylated Alanine-Rich C Kinase SubstrateMolecular BiologyProtein kinase CGlutathione TransferaseBinding SitesCell-Free SystemKinaseChemistryIntracellular Signaling Peptides and ProteinsMembrane ProteinsProteinsCell BiologyHaplorhiniPeptide FragmentsBiochemistryPhosphorylationElectrophoresis Polyacrylamide GelSignal transductionSequence AnalysisSignal TransductionFEBS Letters
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A structural insight into the P1 S1 binding mode of diaminoethylphosphonic and phosphinic acids, selective inhibitors of alanine aminopeptidases

2016

Abstract N′-substituted 1,2-diaminoethylphosphonic acids and 1,2-diaminoethylphosphinic dipeptides were explored to unveil the structural context of the unexpected selectivity of these inhibitors of M1 alanine aminopeptidases (APNs) versus M17 leucine aminopeptidase (LAP). The diaminophosphonic acids were obtained via aziridines in an improved synthetic procedure that was further expanded for the phosphinic pseudodipeptide system. The inhibitory activity, measured for three M1 and one M17 metalloaminopeptidases of different sources (bacterial, human and porcine), revealed several potent compounds (e.g., K i  = 65 nM of 1u for Hs APN). Two structures of an M1 representative (APN from Neisser…

Phosphorous AcidsSwineStereochemistryNeisseria meningitidisCD13 AntigensCrystallography X-RayLigands010402 general chemistry01 natural sciencesAminopeptidaseArticleAminopeptidase NPhosphonic and phosphinic acidsLeucyl AminopeptidaseStructure-Activity RelationshipS1 binding modeDrug DiscoveryAnimalsHumansProtease InhibitorsPharmacologyAlanineBinding Sitesbiology010405 organic chemistryChemistryAminopeptidase NOrganic ChemistryActive siteStructural contextAPN-inhibitor complex structuresDipeptidesGeneral MedicinePhosphinic Acids0104 chemical sciencesMetalloaminopeptidasesPhosphinic Acidsbiology.proteinLeucineSelectivityEuropean Journal of Medicinal Chemistry
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X-ray structure determination of a metastable state of carbonmonoxy myoglobin after photodissociation.

1996

The x-ray structure of carbon monoxide (CO)-ligated myoglobin illuminated during data collection by a laser diode at the wavelength lambda = 690 nm has been determined to a resolution of 1.7 A at T = 36 K. For comparison, we also measured data sets of deoxymyoglobin and CO-ligated myoglobin. In the photon-induced structure the electron density associated with the CO ligand can be described by a tube extending from the iron into the heme pocket over more than 4 A. This density can be interpreted by two discrete positions of the CO molecule. One is close to the heme iron and can be identified to be bound CO. In the second, the CO is dissociated from the heme iron and lies on top of pyrrole ri…

PhotonsBinding SitesPhotolysisMultidisciplinaryFourier AnalysisMyoglobinProtein ConformationLigandPhotodissociationWhalesHemeCrystallography X-Raychemistry.chemical_compoundCrystallographychemistryMetmyoglobinMyoglobinAnimalsMoleculeMetmyoglobinHemeResearch ArticlePyrroleCarbon monoxideProceedings of the National Academy of Sciences
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Computational Chromosome Conformation Capture by Correlation of ChIP-seq at CTCF motifs

2018

Background: Transcription factors (TFs) bind to gene promoters or distal regulatory elements that interact with the promoter via chromatin looping. While the TF binding sites themselves are detected genome-wide by ChIP-seq experiments, it is difficult to associate them regulated genes without information of chromatin looping. Recent experimental techniques such as Hi-C or ChIA-PET measure long-range interactions genome-wide but are experimentally elaborate and have limited resolution. Here, we present Computational Chromosome Conformation Capture by Correlation of ChIP-seq at CTCF motifs (7C). Results: While ChIP-seq was not designed to detect contacts, the formaldehyde treatment in the ChI…

PhysicsChromosome conformation captureCTCFgenetic processesnatural sciencesHuman genomePromoterComputational biologyBinding siteSequence motifTranscription factorChromatin
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Mapping CO diffusion paths in Myoglobin with the Single Sweep Method

2010

The pathways of diffusion and escape of a CO molecule inside and out a myoglobin protein are investigated. Specifically, the three-dimensional potential of mean force (PMF or free energy) of the CO molecule position inside the protein is calculated by using the single-sweep method in concert with fully resolved atomistic simulations in explicit solvent.The results are interpreted under the assumption that the diffusion of the ligand can be modeled as a navigation on the PMF in which the ligand hops between the PMF local minima following the minimum free energy paths (MFEPs) with rates set by the free energy barriers that need to be crossed. We calculate all these quantities --local minima, …

Physics::Biological PhysicsQuantitative Biology::BiomoleculesCo diffusionBiophysicsMolecular physicsMaxima and minimachemistry.chemical_compoundCrystallographyMyoglobinchemistrymyoglobin free energyDocking (molecular)MoleculeSingle sweepBinding sitePotential of mean force
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Functioning of DcuC as the C 4 -Dicarboxylate Carrier during Glucose Fermentation by Escherichia coli

1999

ABSTRACT The dcuC gene of Escherichia coli encodes an alternative C 4 -dicarboxylate carrier (DcuC) with low transport activity. The expression of dcuC was investigated. dcuC was expressed only under anaerobic conditions; nitrate and fumarate caused slight repression and stimulation of expression, respectively. Anaerobic induction depended mainly on the transcriptional regulator FNR. Fumarate stimulation was independent of the fumarate response regulator DcuR. The expression of dcuC was not significantly inhibited by glucose, assigning a role to DcuC during glucose fermentation. The inactivation of dcuC increased fumarate-succinate exchange and fumarate uptake by DcuA and DcuB, suggesting a…

Physiology and MetabolismMolecular Sequence DataMutantStimulationBiologymedicine.disease_causeMicrobiologyBacterial ProteinsFumaratesConsensus SequenceEscherichia colimedicineTranscriptional regulationDicarboxylic AcidsAnaerobiosisPromoter Regions GeneticMolecular BiologyEscherichia coliPsychological repressionDicarboxylic Acid TransportersBinding SitesBase SequenceEscherichia coli ProteinsSuccinatesGene Expression Regulation BacterialKineticsResponse regulatorGlucoseBiochemistryFermentationFermentationEffluxCarrier ProteinsRibosomesJournal of Bacteriology
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