Search results for "porter"

showing 10 items of 920 documents

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
researchProduct

Distant downstream sequence determinants can control N-tail translocation during protein insertion into the endoplasmic reticulum membrane.

2000

We have studied the membrane insertion of ProW, an Escherichia coli inner membrane protein with seven transmembrane segments and a large periplasmic N-terminal tail, into endoplasmic reticulum (ER)-derived dog pancreas microsomes. Strikingly, significant levels of N-tail translocation is seen only when a minimum of four of the transmembrane segments are present; for constructs with fewer transmembrane segments, the N-tail remains mostly nontranslocated and the majority of the molecules adopt an 'inverted' topology where normally nontranslocated parts are translocated and vice versa. N-tail translocation can also be promoted by shortening of the N-tail and by the addition of positively charg…

Models MolecularBioquímicaGlycosylationChromosomal translocationBiologyEndoplasmic ReticulumBiochemistryBacterial ProteinsMembranes (Biologia)MicrosomesEscherichia coliAnimalsInner membranePancreasMolecular BiologyEscherichia coli ProteinsEndoplasmic reticulumMembrane ProteinsSTIM1Periplasmic spaceCell BiologyMolecular biologyTransmembrane proteinCell biologyMembrane proteinMutationCatsMicrosomeATP-Binding Cassette TransportersProteïnesJournal of Biological Chemistry
researchProduct

The Escherichia coli Envelope Stress Sensor CpxA Responds to Changes in Lipid Bilayer Properties

2015

The Cpx stress response system is induced by various environmental and cellular stimuli. It is also activated in Escherichia coli strains lacking the major phospholipid, phosphatidylethanolamine (PE). However, it is not known whether CpxA directly senses changes in the lipid bilayer or the presence of misfolded proteins due to the lack of PE in their membranes. To address this question, we used an in vitro reconstitution system and vesicles with different lipid compositions to track modulations in the activity of CpxA in different lipid bilayers. Moreover, the Cpx response was validated in vivo by monitoring expression of a PcpxP-gfp reporter in lipid-engineered strains of E. coli. Our comb…

Models MolecularCardiolipinsSurface PropertiesRecombinant Fusion ProteinsGreen Fluorescent ProteinsLipid BilayersArabidopsisPhospholipidBiologymedicine.disease_causeBiochemistrychemistry.chemical_compoundBacterial ProteinsGenes ReportermedicineAcholeplasma laidlawiiPhosphorylationLipid bilayerEscherichia coliPlant ProteinsPhosphatidylethanolamineEscherichia coli ProteinsPhosphatidylethanolaminesVesicleGlycosyltransferasesMembrane ProteinsPhosphatidylglycerolsCell biologychemistryMembrane proteinlipids (amino acids peptides and proteins)Protein foldingSignal transductionProtein KinasesProtein Processing Post-TranslationalSignal TransductionBiochemistry
researchProduct

Cytotoxicity of Novel Sulfanilamides Towards Sensitive and Multidrugresistant Leukemia Cells

2014

Novel sulfa Schiff bases were synthesized and characterized by a reaction between aromatic sulfonamides and aromatic aldehydes or heterocyclic ketones in equimolar ratios. Their cytotoxicity was evaluated by the resazurin assay towards human sensitive CCRF-CEM and multidrug-resistant CEM/ADR5000 leukemia cells. Three of the tested compounds viz., 4-(anthracen-9-ylmethyleneamino)-N-(pyrimidin-2-yl)benzenesulfonamide (4), 4-(anthracen-9- ylmethyleneamino)benzenesulfonamide, (5) and 4-((3-phenylallylidene)amino)benzene-sulfonamide, (6) were cytotoxic (IC 50 values: 5.38-19.96 µM). CEM/ADR5000 cells were not cross-resistant to these compounds, indicating activity against otherwise drug-resistan…

Models MolecularCell SurvivalStereochemistryBiochemistrychemistry.chemical_compoundSulfanilamideCell Line TumorSulfanilamidesDrug DiscoverymedicineHumansCytotoxic T cellDoxorubicinATP Binding Cassette Transporter Subfamily B Member 1Homology modelingCytotoxicityPharmacologyLeukemiaChemistryOrganic ChemistryResazurinSulfanilamidemedicine.diseaseProtein Structure TertiaryLeukemiaDoxorubicinDrug Resistance NeoplasmMolecular MedicineVerapamilmedicine.drugCurrent Medicinal Chemistry
researchProduct

Copper(II)-Induced Restructuring of ZnuD, a Zinc(II) Transporter from Neisseria meningitidis.

2019

Cluster 2 (288HDDDNAHAHTH298) from Neisseria meningitidis ZnuD is a flexible loop that captures zinc(II) ions, acting as a "fishing net". We describe its Zn(II) and Cu(II) binding capabilities, focusing on the thermodynamics of such interactions and comparing them with the complexes of the 1MAHHHHHHL9-NH2 region. Copper(II) complexes with the studied ZnuD regions are thermodynamically more stable than the zinc(II) ones-Cu(II) complexes dominate in solution even in close to physiological ratios of the studied metal ions (a 10-fold excess of Zn(II) over Cu(II)). While the binding of native Zn(II) has no significant impact on the structure of its transporter, Cu(II) binding induces a conformat…

Models MolecularConformational changeMetal ions in aqueous solutionchemistry.chemical_elementZincNeisseria meningitidis010402 general chemistry01 natural sciencesInorganic ChemistryBacterial ProteinsHumansProlineAmino Acid SequencePhysical and Theoretical ChemistryCation Transport ProteinsPolyproline helix010405 organic chemistryTransporterCopper0104 chemical sciencesMeningococcal InfectionsCrystallographyZincchemistryHelixThermodynamicsCopperProtein BindingInorganic chemistry
researchProduct

Inhibitors of inducible NO synthase expression: total synthesis of (S)-curvularin and its ring homologues.

2008

(S)-Curvularin and its 13-, 14-, and 16-membered lactone homologues were synthesized through a uniform strategy in which a Kochi oxidative decarboxylation and ring-closing metathesis reactions constitute the key processes. In the evaluation of the anti-inflammatory effects of the synthesized compounds in assays using cells stably transfected with a human iNOS promoter-luciferase reporter gene construct, the 14- and 16-membered homologues showed a slightly higher inhibitory effect towards iNOS promoter activity than curvularin itself. However, the larger ring homologues also exhibited higher cytotoxicity, manifest in downregulated eNOS promoter activity. In contrast, the di-O-acetyl and 4-ch…

Models MolecularDrug Evaluation PreclinicalNitric Oxide Synthase Type IICrystallography X-RayBiochemistryGene Expression Regulation EnzymologicCell LineLactonesEnosDrug DiscoveryHumansGeneral Pharmacology Toxicology and PharmaceuticsEnzyme InhibitorsCytotoxicityPromoter Regions GeneticOxidative decarboxylationPharmacologychemistry.chemical_classificationReporter genebiologyMolecular StructureChemistryOrganic ChemistryTotal synthesisStereoisomerismCurvularinTransfectionbiology.organism_classificationBiochemistryCyclizationMolecular MedicineZearalenoneLactoneHeLa CellsChemMedChem
researchProduct

The Nature of the Stimulus and of the Fumarate Binding Site of the Fumarate Sensor DcuS of Escherichia coli

2005

DcuS is a membrane-associated sensory histidine kinase of Escherichia coli specific for C(4) -dicarboxylates. The nature of the stimulus and its structural prerequisites were determined by measuring the induction of DcuS-dependent dcuB'-'lacZ gene expression. C(4)-dicarboxylates without or with substitutions at C2/C3 by hydrophilic (hydroxy, amino, or thiolate) groups stimulated gene expression in a similar way. When one carboxylate was replaced by sulfonate, methoxy, or nitro groups, only the latter (3-nitropropionate) was active. Thus, the ligand of DcuS has to carry two carboxylate or carboxylate/nitro groups 3.1-3.8 A apart from each other. The effector concentrations for half-maximal i…

Models MolecularMagnetic Resonance SpectroscopyHistidine KinaseRecombinant Fusion ProteinsMolecular Sequence Datamedicine.disease_causeBiochemistryCitric AcidStructure-Activity Relationshipchemistry.chemical_compoundFumaratesEscherichia colimedicineDicarboxylic AcidsAmino Acid SequenceCarboxylatePhosphorylationBinding siteKinase activityTartratesMolecular BiologyEscherichia coliPeptide sequenceDicarboxylic Acid TransportersBinding SitesChemistryEscherichia coli ProteinsAutophosphorylationHistidine kinaseGene Expression Regulation BacterialCell BiologyNitro CompoundsPeptide FragmentsEnzyme ActivationLac OperonBiochemistryMutagenesis Site-DirectedPropionatesProtein KinasesSequence AlignmentBinding domainJournal of Biological Chemistry
researchProduct

Oxytocin receptors and cholesterol: interaction and regulation.

2000

Cholesterol affects the ligand binding function of the oxytocin receptor in a highly specific manner. While the structurally-related cholecystokinin receptor shows a strong correlation between the membrane fluidity and its binding function, the oxytocin receptor behaves differently. A stringent and unique requirement of the affinity state of the oxytocin receptor for structural features of the sterol molecule has been found. The molecular requirements differ both from those postulated for sterol-phospholipid interactions and from those known to be necessary for the activity of other proteins. Employing a new detergent-free subcellular fractionation protocol, a two-fold enrichment of the oxy…

Models MolecularMembrane FluidityCaveolin 1Green Fluorescent ProteinsBiologyKidneyTransfectionCholecystokinin receptorCaveolinsGenes ReportermedicineMembrane fluidityExtracellularHumansReceptorCells CulturedBinding SitesCholesterol bindingCell MembraneMembrane ProteinsGeneral MedicineOxytocin receptorRecombinant ProteinsLuminescent ProteinsMembraneCholesterolOxytocinBiochemistryReceptors OxytocinBiophysicsIndicators and ReagentsReceptors CholecystokininSteroidshormones hormone substitutes and hormone antagonistsmedicine.drugExperimental physiology
researchProduct

Antigen processing influences HIV-specific cytotoxic T lymphocyte immunodominance

2016

Udgivelsesdato: 2009-May-03 Although cytotoxic T lymphocytes (CTLs) in people infected with human immunodeficiency virus type 1 can potentially target multiple virus epitopes, the same few are recognized repeatedly. We show here that CTL immunodominance in regions of the human immunodeficiency virus type 1 group-associated antigen proteins p17 and p24 correlated with epitope abundance, which was strongly influenced by proteasomal digestion profiles, affinity for the transporter protein TAP, and trimming mediated by the endoplasmatic reticulum aminopeptidase ERAAP, and was moderately influenced by HLA affinity. Structural and functional analyses demonstrated that proteasomal cleavage 'prefer…

Models MolecularProteasome Endopeptidase ComplexHIV AntigensMolecular Sequence DataImmunologyAntigen presentationHIV Core Protein p24HIV InfectionsImmunodominanceMajor histocompatibility complexgag Gene Products Human Immunodeficiency VirusEpitopeEvolution MolecularMajor Histocompatibility ComplexLeucyl Aminopeptidase03 medical and health sciences0302 clinical medicineAntigenHumansImmunology and AllergyCytotoxic T cellAmino Acid Sequence030304 developmental biologyAntigen Presentation0303 health sciencesHLA-A AntigensbiologyImmunodominant EpitopesAntigen processingVirology3. Good healthCTL*MutationHIV-1biology.proteinATP-Binding Cassette TransportersProtein BindingT-Lymphocytes Cytotoxic030215 immunologyRETROVIROLOGY
researchProduct

When two turn into one: evolution of membrane transporters from half modules

2014

Abstract The recently increasing number of atomic structures for active transporters has not only revealed strong conservation in the architecture of sequence-unrelated transporter families, but also identified a unifying element called the ‘inverted repeat topology,’ which is found in nearly all transporter folds to date. Indeed, most membrane transporters consist of two or more domains with similar structure, so-called repeats. It is tempting to speculate that transporters have evolved by duplication of one repeat followed by gene fusion and modification events. An intriguing question is, whether recent genes encoding such a ‘half-transporter’ still exist as independent folding units. Alt…

Models MolecularProtein FoldingbiologyProtein familyProtein ConformationMembrane transport proteinInverted repeatClinical BiochemistryMembrane Transport ProteinsTransporterBiochemistryEvolution MolecularProtein structureBiochemistryEvolutionary biologyGene duplicationbiology.proteinAnimalsHumansProtein foldingMolecular BiologyGeneBiological Chemistry
researchProduct