Search results for "Subunit"

showing 10 items of 513 documents

Cloning of Sponge (Geodia cydonium) and Tunicate (Botryllus schlosseri) Proteasome Subunit Epsilon (PRCE): Implications about the Vertebrate MHC-Enco…

1996

Proteasomes are large protein complexes that play a major role in selective degradation of intracellular proteins. Eukaryotes feature seven different alpha and beta subunits. Two of the vertebrate housekeeping beta-subunits have MHC-encoded homologues that can substitute for the housekeeping counterparts upon interferon-gamma induction. In the present study we report the cloning of invertebrate beta-subunit proteasome epsilon (PRCE), from the marine sponge Geodia cydonium and from the colonial tunicate Botryllus schlosseri. Sequence comparisons revealed that the sponge and tunicate proteins are strikingly similar to vertebrate and yeast PRCEs and their MHC-linked counterparts the PRCCs (als…

Proteasome Endopeptidase ComplexDNA ComplementaryProtein subunitMolecular Sequence DataBiophysicsSaccharomyces cerevisiaeBotryllus schlosseriPolymerase Chain ReactionBiochemistryMiceMultienzyme ComplexesConsensus SequenceBotanyAnimalsHumansAmino Acid SequenceUrochordataCloning MolecularProtein precursorMolecular BiologyPhylogenyDNA Primerschemistry.chemical_classificationCloningBase SequenceSequence Homology Amino AcidbiologyProteinsCell Biologybiology.organism_classificationYeastPoriferaRatsAmino acidTunicateCell biologyCysteine EndopeptidaseschemistryProteasomeVertebratesChickensBiochemical and Biophysical Research Communications
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Combining two mutations of human interleukin-6 that affect gp130 activation results in a potent interleukin-6 receptor antagonist on human myeloma ce…

1995

The pleiotropic cytokine interleukin-6 (IL-6) interacts with the specific ligand binding subunit (IL-6R alpha) of the IL-6 receptor, and this complex associates with the signal-transducing subunit gp130 (IL-6R beta). Human IL-6 acts on human and murine cells, whereas murine IL-6 is only active on murine cells. The construction of a set of chimeric human/murine IL-6 proteins has recently allowed us to define a region (residues 43-55) within the human IL-6 protein, which is important for the interaction with gp130. Subdividing this region shows that mainly residues 50-55 of the human IL-6 are necessary for this interaction. Recently, another human IL-6 double mutant (Q159E and T162P) showed r…

Protein ConformationProtein subunitmedicine.medical_treatmentMutantMolecular Sequence DataBiologyBiochemistryMiceAntigenAntigens CDmedicineCytokine Receptor gp130Tumor Cells CulturedAnimalsHumansPoint MutationInterleukin 6ReceptorMolecular BiologyMembrane GlycoproteinsBase SequenceInterleukin-6Wild typeCell BiologyReceptors InterleukinGlycoprotein 130Molecular biologyReceptors Interleukin-6CytokineOligodeoxyribonucleotidesbiology.proteinMultiple MyelomaThe Journal of biological chemistry
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Identification of Single Amino Acid Residues of Human IL-6 Involved in Receptor Binding and Signal Initiation

1996

The pleiotropic cytokine interleukin-6 (IL-6) has been predicted to be a protein with four antiparallel alpha-helices. On target cells, IL-6 interacts with a specific ligand binding receptor subunit (IL-6R), and this complex associates with the signal-transducing subunit gp130. Human IL-6 acts on human and murine cells, whereas murine IL-6 is only active on murine cells. The construction of chimeric human/murine IL-6 proteins has allowed us to define a region (residues 77-95, region 2c) within the human IL-6 protein that is important for IL-6R binding and a region (residues 50-55, region 2a2) that is important for IL-6R dependent gp130 interaction. Guided by sequence alignment and molecular…

Protein ConformationRecombinant Fusion ProteinsProtein subunitMolecular Sequence DataImmunologySequence alignmentPlasma protein bindingBiologyLigandsMiceStructure-Activity RelationshipProtein structureAntigens CDVirologyCytokine Receptor gp130AnimalsHumansPoint MutationAmino Acid SequenceAmino AcidsReceptorPeptide sequenceMembrane GlycoproteinsInterleukin-6Receptors InterleukinCell BiologyGlycoprotein 130Receptors Interleukin-6BiochemistryMutagenesis Site-DirectedSignal transductionSequence AlignmentProtein BindingSignal TransductionJournal of Interferon & Cytokine Research
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Influence of antibody binding on oxygen binding behavior of Panulirus interruptus hemocyanin

1997

Oxygen binding behavior of monomeric subunit a and the hexameric form of this subunit of hemocyanin of Panulirus interruptus is influenced by the binding of various monoclonal antibodies. These antibodies react with other surface parts of the subunit than its second domain in which the oxygen binding site is located. The influence of three monoclonal antibodies and their antigen binding fragments (F-ab) has been investigated. Two antibodies increase the oxygen affinity of monomeric hemocyanin from that observed in its low affinity T-state, while the third has little influence on this property. F-ab fragments abolish almost completely the cooperativity of oxygen binding by the hexameric hemo…

Protein ConformationStereochemistrymedicine.drug_classProtein subunitmedicine.medical_treatmentcooperativityBiophysicsCooperativityPlasma protein bindingmacromolecular substancesMonoclonal antibodyBiochemistryEpitopesImmunoglobulin Fab FragmentsProtein structureSUBUNIT-AStructural BiologyAMINO-ACID SEQUENCEGeneticsmedicineAnimalsCRYSTAL-STRUCTUREMolecular BiologyPanulirus interruptusChemistryImmunoglobulin Fab FragmentsAntibodies MonoclonalHemocyaninCell BiologyNephropidaeOxygenBiochemistryRESOLUTIONHemocyaninsoxygen bindingmonoclonal antibodieshemocyaninOxygen bindingProtein Binding
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Subunits composition and allosteric control in Carcinus aestuarii hemocyanin

1998

Carcinus aestuarii hemocyanin (Hc) exists in two aggregation forms at pH 7.5 and 20 mM Ca2+: 24S accounting for 90% of total hemocyanin and 16S accounting for 10%. Removal of metal cations by EDTA at neutral pH causes the complete dissociation of 24S hemocyanin into two different 16S. At pH 9.2, 24S hemocyanin dissociates into a pH stable 16S and a 5S component. The 5S component consists of three monomeric fractions named CaeSS1 (10%), CaeSS2 (50%) and CaeSS3 (40%); the latter fraction consisting of two isoforms. The fractions CaeSS1, CaeSS2 and CaeSS3 have been studied as far as their reassociation properties to form hexamers are concerned. We investigated the oxygen-binding properties of …

Protein ConformationStereochemistrymedicine.medical_treatmentProtein subunitAllosteric regulationHemocyaninBiochemistryAllosteric interactionchemistry.chemical_compoundProtein structureOxygen bindingAllosteric RegulationCrustaceaMetalloproteinsmedicineMetalloproteinAnimalschemistry.chemical_classificationHemocyanin; Oxygen binding; Allosteric interaction; OxygenbiologyHemocyaninHydrogen-Ion Concentrationbiology.organism_classificationOxygenCarcinus aestuariiMonomerBiochemistrychemistryHemocyaninsChromatography GelElectrophoresis Polyacrylamide GelOxygen bindingProtein Binding
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Molecular mass of macromolecules and subunits and the quaternary structure of hemoglobin from the microcrustacean Daphnia magna

2006

The molecular masses of macromolecules and subunits of the extracellular hemoglobin from the fresh-water crustacean Daphnia magna were determined by analytical ultracentrifugation, multiangle laser light scattering and electrospray ionization mass spectrometry. The hemoglobins from hypoxia-incubated, hemoglobin-rich and normoxia-incubated, hemoglobin-poor Daphnia magna were analyzed separately. The sedimentation coefficient of the macromolecule was 17.4 +/- 0.1 S, and its molecular mass was 583 kDa (hemoglobin-rich animals) determined by AUC and 590.4 +/- 11.1 kDa (hemoglobin-rich animals) and 597.5 +/- 49 kDa (hemoglobin-poor animals), respectively, determined by multiangle laser light sca…

Protein DenaturationChromatography GasGlycosylationLightMacromolecular SubstancesProtein ConformationElectrospray ionizationProtein subunitDaphnia magnaMultiangle light scatteringBiologyBiochemistryHemoglobinsImaging Three-DimensionalAnimalsScattering RadiationProtein Structure QuaternaryMolecular BiologyChromatography High Pressure LiquidChromatographyMolecular massLasersfungiCell BiologyHemoglobin Subunitsbiology.organism_classificationMolecular WeightProtein SubunitsDaphniaFemaleProtein quaternary structureHemoglobinFEBS Journal
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Linked Analysis of Large Cooperative, Allosteric Systems: The Case of the Giant HBL Hemoglobins

2008

Homotropic and heterotropic allosteric interactions are important mechanisms that regulate protein function. These mechanisms depend on the ability of oligomeric protein complexes to adopt different conformations and to transmit conformation-linked signals from one subunit of the complex to the neighboring ones. An important step in understanding the regulation of protein function is to identify and characterize the conformations available to the protein complex. This task becomes increasingly challenging with increasing numbers of interacting binding sites. However, a large number of interacting binding sites allows for high homotropic interactions (cooperativity) and thus represents the m…

Protein functionOrder (biology)BiochemistryHexagonal crystal systemBilayerProtein subunitAllosteric regulationBiophysicsCooperativityBiologyBinding site
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Effects of sulindac sulfide on the membrane architecture and the activity of gamma-secretase.

2007

gamma-Secretase is a membrane-embedded multi-protein complex that catalyzes the final cut of the Alzheimer's disease-related amyloid precursor protein (APP) to amyloid-beta peptides of variable length (37-43 amino acids) via an unusual intramembrane cleavage. Recent findings propose that some commonly used non-steroidal anti-inflammatory drugs (NSAIDs) have the ability to modulate specifically gamma-secretase activity without inhibiting the enzyme as a whole. These drugs may shift the processing of APP from the longer amyloid-beta 42 peptide towards shorter, less fibrillogenic and less toxic amyloid-beta species. We hypothesize that gamma-secretase activity, as an enzyme that is strictly as…

Protein subunitBlotting WesternPeptideCHO CellsSarcoplasmic Reticulum Calcium-Transporting ATPasesCellular and Molecular NeuroscienceAmyloid beta-Protein PrecursorCricetulusMembrane MicrodomainsSulindacCricetinaemental disordersAmyloid precursor proteinPresenilin-1AnimalsHumansLipid raftCells CulturedPharmacologychemistry.chemical_classificationbiologyAnti-Inflammatory Agents Non-SteroidalCell MembraneP3 peptideAmino acidMembraneBiochemistrychemistrybiology.proteinBiophysicsAmyloid Precursor Protein SecretasesAmyloid precursor protein secretaseNeuropharmacology
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Recombinant functional multidomain hemoglobin from the gastropod Biomphalaria glabrata

2011

The extracellular hemoglobin multimer of the planorbid snail Biomphalaria glabrata, intermediate host of the human parasite Schistosoma mansoni, is presumed to be a 1.44 MDa complex of six 240 kDa polypeptide subunits, arranged as three disulfide-bridged dimers. The complete amino acid sequence of two subunit types (BgHb1 and BgHb2), and the partial sequence of a third type (BgHb3) are known. Each subunit encompasses 13 paralogus heme domains, and N-terminally a smaller plug domain responsible for subunit dimerization. We report here the recombinant expression of different functional fragments of BgHb2 in Escherichia coli, and of the complete functional subunits BgHb1 and BgHb2 in insect ce…

Protein subunitClinical BiochemistryCooperativitymedicine.disease_causeBiochemistrylaw.inventionHemoglobinschemistry.chemical_compoundlawGeneticsmedicineAnimalsHumansBiomphalaria glabrataProtein Structure QuaternaryMolecular BiologyEscherichia coliPeptide sequenceHemeBiomphalariabiologySchistosoma mansoniCell Biologybiology.organism_classificationRecombinant ProteinsOxygenProtein SubunitsBiochemistrychemistryRecombinant DNAOxygen bindingIUBMB Life
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Direct evidence that FK506 inhibition of FcεRI-mediated exocytosis from RBL mast cells involves calcineurin

1998

eRI-mediated exocytosis of preformed mediators from mast cells and basophils (e.g. histamine, serotonin, beta-hexosaminidase) is sensitive to the immunosuppressants cyclosporin A and FK506 (IC 50 200 and 4 n M , respectively) but not rapamycin. The mechanism of inhibition does not appear to involve tyrosine phosphorylation, hydrolysis of inositol phosphates or calcium flux. Here we report experiments using a molecular approach to assess the role of calcineurin, a serine/threonine phosphatase thought to be the primary pharmacological target of these drugs. Calcineurin’s activity requires association of its catalytic (A) subunit with an intrinsic regulatory (B) subunit. We hypothesized that c…

Protein subunitDermatologyBiologyTransfectionSensitivity and SpecificityCell DegranulationExocytosisTacrolimusExocytosischemistry.chemical_compoundCyclosporin aCalcium fluxTumor Cells CulturedmedicineAnimalsMast CellsDose-Response Relationship DrugReceptors IgECalcineurinTyrosine phosphorylationGeneral MedicineMast cellRatsCell biologyCalcineurinElectroporationmedicine.anatomical_structureLeukemia Basophilic AcutechemistryBiochemistryImmunosuppressive AgentsHistamineArchives of Dermatological Research
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