Search results for "binding site"

showing 10 items of 856 documents

Mode of primary binding to target membranes and pore formation induced by Vibrio cholerae cytolysin (hemolysin).

1997

Vibrio cholerae cytolysin (VCC) is produced by many non-choleratoxigenic strains of V. cholerae, and possibly represents a relevant pathogenicity determinant of these bacteria. The protein is secreted as a pro-toxin that is proteolytically cleaved to yield the active toxin with a molecular mass of approximately 63 kDa. We here describe a simple procedure for preparative isolation of mature VCC from bacterial culture supernatants, and present information on its mode of binding and pore formation in biological membranes. At low concentrations, toxin monomers interact with a high-affinity binding site on highly susceptible rabbit erythrocytes. This as yet unidentified binding site is absent on…

Pore-forming toxinBinding SitesToxinCytotoxinsErythrocyte MembraneMolecular Sequence DataAerolysinHemolysinBiologymedicine.disease_causeBiochemistryTransmembrane proteinMolecular WeightBiochemistryVibrio choleraemedicineAnimalsHumansCytolysinAmino Acid SequenceRabbitsBinding siteVibrio choleraeEuropean journal of biochemistry
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Application of 3-Quinolinoyl Picket Porphyrins to the Electroreduction of Dioxygen to Water: Mimicking the Active Site of Cytochromec Oxidase

2001

International audience

PorphyrinsHemeproteinReducing agentIronchemistry.chemical_elementPhotochemistryElectrochemistry[ CHIM ] Chemical SciencesBiochemistryOxygenElectron Transport Complex IVO-O activationcytochrome c oxidase[CHIM]Chemical SciencesCytochrome c oxidaseBinding siteMolecular BiologyComputingMilieux_MISCELLANEOUSBinding SitesbiologyChemistryMolecular MimicryOrganic ChemistryActive siteElectron Transport Complex IVheme proteinsoxidoreductasesOxygenelectrochemistryReducing Agentsbiology.proteinMolecular MedicineIndicators and ReagentsSpectrophotometry UltravioletOxidation-ReductionCopperChemBioChem
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Orphan nuclear receptor binding site in the human inducible nitric oxide synthase promoter mediates responsiveness to steroid and xenobiotic ligands

2002

Constitutive androstane receptor (CAR) and pregnane X receptor (PXR) are members of the nuclear receptor superfamily that regulate target gene transcription in a ligand-dependent manner. CAR and PXR have a rather broad, overlapping set of ligands that range from natural steroids to xenobiotics and also recognize similar DNA binding sites, referred to as response elements (REs), primarily in promoter regions of cytochrome P450 (CYP) genes. In this study, a CAR and PXR RE, composed of a direct repeat of two GGTTCA motifs in a distance of 4 nucleotides (DR4), was identified in the promoter of the human inducible nitric oxide (NO) synthase (iNOS) gene, which is the first nuclear receptor bindin…

Pregnane X receptorCell BiologyRetinoid X receptorBiologydigestive systemBiochemistryCalcitriol receptorCell biologyBiochemistryNuclear receptorDownregulation and upregulationConstitutive androstane receptorBinding siteReceptorMolecular BiologyJournal of Cellular Biochemistry
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Functional characterization of two melanocortin (MC) receptors in lamprey showing orthology to the MC1 and MC4 receptor subtypes

2007

Abstract Background The melanocortin (MC) receptors have a key role in regulating body weight and pigmentation. They belong to the rhodopsin family of G protein-coupled receptors (GPCRs). The purpose of this study was to identify ancestral MC receptors in agnathan, river lamprey. Results We report cloning of two MC receptors from river lamprey. The lamprey receptors, designated MCa and MCb, showed orthology to the MC1 and MC4 receptor subtypes, respectively. The molecular clock analysis suggested that lamprey MC receptor genes were not duplicated recently and diverged from each other more than 400 MYR ago. Expression and pharmacological characterization showed that the lamprey MCa receptor …

Pro-OpiomelanocortinSecond Messenger SystemsGene DuplicationProtein Interaction MappingCyclic AMPPetromyzonReceptorPhylogenyCell Line TransformedSkinGeneticsbiologyReceptors MelanocortinMelanocortin 3 receptorCell biologyOrgan SpecificityRhodopsinReceptor Melanocortin Type 4HagfishesMelanocortinReceptor Melanocortin Type 1Protein BindingResearch ArticleEvolutionRecombinant Fusion ProteinsMolecular Sequence DataBinding CompetitivePeptides CyclicEvolution Moleculargamma-MSHAdrenocorticotropic HormoneSpecies SpecificityMelanocortin receptorbeta-MSHQH359-425AnimalsHumansAmino Acid SequenceEcology Evolution Behavior and SystematicsGene LibraryG protein-coupled receptorBinding SitesSequence Homology Amino AcidFuguLampreybiology.organism_classificationPeptide FragmentsVisceraalpha-MSHbiology.proteinCosyntropinSequence Alignmenthuman activitiesBMC Evolutionary Biology
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MYC and EGR1 synergize to trigger tumor cell death by controlling NOXA and BIM transcription upon treatment with the proteasome inhibitor bortezomib

2014

The c-MYC (MYC afterward) oncogene is well known for driving numerous oncogenic programs. However, MYC can also induce apoptosis and this function of MYC warrants further clarification. We report here that a clinically relevant proteasome inhibitor significantly increases MYC protein levels and that endogenous MYC is necessary for the induction of apoptosis. This kind of MYC-induced cell death is mediated by enhanced expression of the pro-apoptotic BCL2 family members NOXA and BIM. Quantitative promoter-scanning chromatin immunoprecipitations (qChIP) further revealed binding of MYC to the promoters of NOXA and BIM upon proteasome inhibition, correlating with increased transcription. Both pr…

Programmed cell deathTranscription GeneticEGR1ApoptosisBiologyBortezomibProto-Oncogene Proteins c-mycMicehemic and lymphatic diseasesCell Line TumorProto-Oncogene ProteinsGeneticsmedicineAnimalsPromoter Regions GeneticTranscription factorCells CulturedEarly Growth Response Protein 1Zinc finger transcription factorBinding SitesOncogeneBcl-2-Like Protein 11Genes p16Gene regulation Chromatin and EpigeneticsMembrane ProteinsPromoterGenes p53Boronic AcidsChromatinddc:Gene Expression Regulation NeoplasticProto-Oncogene Proteins c-bcl-2PyrazinesCancer researchProteasome inhibitorApoptosis Regulatory ProteinsProteasome Inhibitorsmedicine.drug
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Development of a second generation of inhibitors of microsomal prostaglandin E synthase 1 expression bearing the γ-hydroxybutenolide scaffold

2008

Petrosaspongiolide M (PM), a marine sesterterpene metabolite bearing the gamma-hydroxybutenolide scaffold and displaying a potent inhibitory activity toward PLA(2) enzyme, was selected by us as an attractive target in order to explore its mechanism of action at molecular level. In the course of our investigations we decided to synthetically modify the parent compound to clarify the structural determinants responsible for the activity; in fact, very recently, our research group reported the synthesis and the pharmacological properties of a first collection of PM analogues generated by Ludi approach. The synthesized compounds showed a poor or moderate activity toward PLA(2) enzymes, neverthel…

Prostaglandin AntagonistsStereochemistryMetaboliteClinical BiochemistryAnti-Inflammatory AgentsPharmaceutical ScienceIsomeraseProstaglandin E synthaseBiochemistryChemical synthesisCell LineMiceStructure-Activity Relationshipchemistry.chemical_compound4-ButyrolactoneMicrosomesDrug DiscoverymedicineAnimalsEnzyme InhibitorsProstaglandin E2Molecular BiologyProstaglandin-E Synthaseschemistry.chemical_classificationBinding SitesbiologyChemistryMacrophagesOrganic ChemistryIntramolecular OxidoreductasesPhospholipases A2EnzymeGene Expression RegulationMechanism of actionBiochemistryCyclooxygenase 2Enzyme inhibitorbiology.proteinMolecular Medicinelipids (amino acids peptides and proteins)medicine.symptommedicine.drugBioorganic & Medicinal Chemistry
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Inhibition of glycosaminoglycan modification of perlecan domain I by site-directed mutagenesis changes protease sensitivity and laminin-1 binding act…

1998

AbstractGlycosaminoglycan attachment to perlecan domain I (173 residues) was completely prevented by site-directed mutagenesis of Ser-65, Ser-71 and Ser-76 as shown by recombinant production in mammalian cells. This did not interfere with the proper folding of the domain's SEA module but enhanced its sensitivity to neutral proteases. Lack of substitution also abolished binding to the two major heparin binding sites of laminin-1.

ProteasesBasement membraneRecombinant proteinmedicine.medical_treatmentMolecular Sequence DataBiophysicsPerlecanBiochemistrySubstrate SpecificityStructural BiologyLamininEndopeptidasesGeneticsmedicineAnimalsAmino Acid SequenceBinding siteSite-directed mutagenesisMolecular BiologyGlycosaminoglycansSite-directed mutagenesisBinding SitesProteasebiologyChemistryMutagenesisCell BiologyRecombinant ProteinsBiochemistryProteoglycanProteoglycanProteolysisMutagenesis Site-Directedbiology.proteinProteoglycansHeparitin SulfateLamininHeparan Sulfate ProteoglycansProtein BindingFEBS Letters
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Role of toxin activation on binding and pore formation activity of the Bacillus thuringiensis Cry3 toxins in membranes of Leptinotarsa decemlineata (…

2004

AbstractBinding and pore formation constitute key steps in the mode of action of Bacillus thuringiensis δ-endotoxins.In this work, we present a comparative analysis of toxin-binding capacities of proteolytically processed Cry3A, Cry3B and Cry3C toxins to brush border membranes (BBMV) of the Colorado potato beetle Leptinotarsa decemlineata (CPB), a major potato coleopteran-insect pest. Competition experiments showed that the three Cry3 proteolytically activated toxins share a common binding site. Also heterologous competition experiments showed that Cry3Aa and Cry3Ca toxins have an extra binding site that is not shared with Cry3Ba toxin. The pore formation activity of the three different Cry…

ProteasesBrush borderBacterial ToxinsBacillus thuringiensisBiophysicsmedicine.disease_causeBinding CompetitiveBiochemistryHemolysin ProteinsBacterial ProteinsBacillus thuringiensisEndopeptidasesmedicineAnimalsProtoxin activationBinding siteProtein PrecursorsChymotrypsinBinding SitesbiologyBacillus thuringiensis ToxinsMicrovilliToxinColorado potato beetleCell MembranefungiCell Biologybiology.organism_classificationTrypsinColeopteraEndotoxinsBiochemistryMode of actionbiology.proteinmedicine.drugBiochimica et Biophysica Acta (BBA) - Biomembranes
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A membrane associated metalloprotease cleaves Cry3Aa Bacillus thuringiensis toxin reducing pore formation in Colorado potato beetle brush border memb…

2007

AbstractInsect proteases are implicated in Bacillus thuringiensis insecticidal proteins mode of action determining toxin specificity and sensitivity. Few data are available on the involvement of proteases in the later steps of toxicity such as protease interaction with toxin–receptor complexes and the pore formation process. In this study, a Colorado potato beetle (CPB) midgut membrane metalloprotease was found to be involved in the proteolytic processing of Cry3Aa. Interaction of Cry3Aa with BBMV membrane proteases resulted in a distinct pattern of proteolysis. Cleavage was demonstrated to occur in protease accessible regions of domain III and was specifically inhibited by the metalloprote…

ProteasesCell Membrane PermeabilityPore formationProteolysismedicine.medical_treatmentBacterial ToxinsBacillus thuringiensisBiophysicsInsecticidal toxinBiochemistryCry3Aa proteolysisHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineColorado potato beetleAnimalsMetalloprotease inhibitorMetalloproteinaseBinding SitesProteaseBacillus thuringiensis ToxinsMicrovillibiologymedicine.diagnostic_testSecretory VesiclesAcetohydroxamic acidColorado potato beetleCell Biologybiology.organism_classificationProteaseColeopteraEndotoxinsModels ChemicalBiochemistryPorosityProtein Bindingmedicine.drugBiochimica et Biophysica Acta (BBA) - Biomembranes
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Proteolytic Processing ofBacillus thuringiensisCryIIIA Toxin and Specific Binding to Brush-Border Membrane Vesicles ofLeptinotarsa decemlineata(Color…

1996

Abstract The mode of action of Bacillus thuringiensis insecticidal proteins in lepidopteran insects is known to involve five steps: ingestion, solubilization, protease activation, binding to midgut membrane receptors, and disruption of the intestinal membrane. Two of these steps, protease activation and binding to midgut membrane receptors, have been analyzed in the major potato pest, the coleoptera Leptinotarsa decemlineata (Colorado potato beetle). Unlike recently proposed, after treatment of the coleopteran-specific B. thuringiensis toxin CryIIIA with gut content from the Colorado potato beetle, a 42-kDa processing polypeptide has been identified. The study of binding to midgut membrane …

ProteasesChymotrypsinProteasebiologyHealth Toxicology and Mutagenesismedicine.medical_treatmentfungiColorado potato beetleBiological pest controlfood and beveragesMidgutGeneral Medicinebiology.organism_classificationBiochemistryBacillus thuringiensisbiology.proteinmedicineBinding siteAgronomy and Crop SciencePesticide Biochemistry and Physiology
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