Search results for " quaternary"

showing 10 items of 148 documents

Heterodimerization of Two Pathological Mutants Enhances the Activity of Human Phosphomannomutase2

2015

The most frequent disorder of glycosylation is due to mutations in the gene encoding phosphomannomutase2 (PMM2-CDG). For this disease, which is autosomal and recessive, there is no cure at present. Most patients are composite heterozygous and carry one allele encoding an inactive mutant, R141H, and one encoding a hypomorphic mutant. Phosphomannomutase2 is a dimer. We reproduced composite heterozygosity in vitro by mixing R141H either with the wild type protein or the most common hypomorphic mutant F119L and compared the quaternary structure, the activity and the stability of the heterodimeric enzymes. We demonstrated that the activity of R141H/F119L heterodimers in vitro, which reproduces t…

Genetics and Molecular Biology (all)HeterozygoteProtein StructureGlycosylationMutantlcsh:MedicineGlucose-6-PhosphateBiologymedicine.disease_causeBiochemistryQuaternaryCongenital Disorders of GlycosylationProtein structuremedicineAlleles; Congenital Disorders of Glycosylation; Dimerization; Glucose-6-Phosphate; Glycosylation; Heterozygote; Humans; Mutation; Phosphorylation; Phosphotransferases (Phosphomutases); Protein Structure Quaternary; Agricultural and Biological Sciences (all); Biochemistry Genetics and Molecular Biology (all); Medicine (all)HumansPhosphorylationAlleleProtein Structure Quaternarylcsh:ScienceGeneAllelesMutationMultidisciplinaryMedicine (all)lcsh:RWild typeMolecular biologyEnzyme structureProteostasisAgricultural and Biological Sciences (all)heterodimresPhosphotransferases (Phosphomutases)Mutationlcsh:QCDG-PMM2DimerizationResearch ArticlePLOS ONE
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The inhibition of glycerol permeation through aquaglyceroporin-3 induced by mercury(II)

2016

Mercurial compounds are known to inhibit water permeation through aquaporins (AQPs). Although in the last years some hypotheses were proposed, the exact mechanism of inhibition is still an open question and even less is known about the inhibition of the glycerol permeation through aquaglyceroporins. Molecular dynamics (MD) simulations of human aquaporin-3 (AQP3) have been performed up to 200 ns in the presence of Hg2+ ions. For the first time, we have observed the unbiased passage of a glycerol molecule from the extracellular to cytosolic side. Moreover, the presence of Hg2+ ions covalently bound to Cys40 leads to a collapse of the aromatic/arginine selectivity filter (ar/R SF), blocking th…

Glycerol0301 basic medicineMolecular dynamicCell Membrane PermeabilityBiochemistryProtein Structure Secondarychemistry.chemical_compoundGLPFCOORDINATIONCRYSTALEscherichia coli ProteinsPermeationBiochemistryCovalent bondSettore CHIM/03 - Chimica Generale E InorganicaPhosphatidylcholinesCOMPLEXESProtein BindingSTRUCTURAL BASISCations DivalentPlasmodium falciparumAquaporinCYSTEINE-189Molecular Dynamics SimulationMolecular dynamicsAquaporinsWATER CHANNELInorganic Chemistry03 medical and health sciencesEscherichia coliGlycerolExtracellularHumansMoleculePERMEABILITYProtein Structure QuaternaryAquaporin 3Binding SitesAQUAPORIN INHIBITIONWaterBiological TransportMembranes ArtificialAquaglyceroporinMercurySIMULATIONSProtein Structure TertiaryCytosolWater permeation030104 developmental biologyAquaglyceroporinschemistryStructural Homology ProteinBiophysicsGlycerol permeationJournal of Inorganic Biochemistry
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Interaction of wild-type and naturally occurring deleted variants of hepatitis B virus core polypeptides leads to formation of mosaic particles

2000

AbstractThe simultaneous presence of hepatitis B virus (HBV) genomes carrying wild-type (wt) and in-frame deleted variants of the HBV core gene has been identified as a typical feature of HBV-infected renal transplant patients with severe liver disease. To investigate possible interactions of wt and deleted core polypeptides a two-vector Escherichia coli expression system ensuring their concomitant synthesis has been developed. Co-expression of wt and a mutant core lacking 17 amino acid residues (77–93) within the immunodominant region led to the formation of mosaic particles, whereas the mutant alone was incapable of self-assembly.

Hepatitis B virusBlotting WesternMutantBiophysicsBiologymedicine.disease_causeBiochemistryGenomeHepatitis B virus PRE betaLiver diseaseStructural BiologyEscherichia coliGeneticsmedicineProtein Structure QuaternaryMolecular BiologyEscherichia coliSequence DeletionHepatitis B virusImmunodominant EpitopesHepatitis B virus coreViral Core ProteinsVirus AssemblyWild typeGenetic VariationCell Biologymedicine.diseaseDimer formationHepatitis B Core AntigensPrecipitin TestsVirologyMolecular biologyRecombinant ProteinsMosaic particleMicroscopy ElectronPeptidesDimerizationC gene deletionProtein BindingFEBS Letters
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Mosaic particles formed by wild-type hepatitis B virus core protein and its deletion variants consist of both homo- and heterodimers.

2003

AbstractCo-expression in Escherichia coli of wild-type (wt) hepatitis B virus core protein (HBc) and its naturally occurring variants with deletions at amino acid positions 77–93 or 86–93 leads to formation of mosaic particles, which consist of three dimer subunit compositions. These compositions are wt/variant HBc heterodimers and two types of homodimers, formed by wt HBc or the variant HBc themselves. Mosaic particles were found also when both HBc deletion variants 77–93 and 86–93 were co-expressed in E. coli. These findings are discussed in terms of their significance for hepatitis B virus pathogenesis and prospective use of mosaic particles in vaccine development.

Hepatitis B virusvirusesProtein subunitDimerBiophysicsExpressionPlasma protein bindingBiologymedicine.disease_causeMosaic particlesBiochemistrychemistry.chemical_compoundHepatitis B virus core proteinProtein structureStructural Biologyparasitic diseasesGeneticsmedicineHepatitis B VaccinesCloning MolecularProtein Structure QuaternaryMolecular BiologyEscherichia coliSequence Deletionchemistry.chemical_classificationHepatitis B virusViral Core ProteinsWild typevirus diseasesGenetic VariationCell BiologyHepatitis BDimer formationVirologyMolecular biologydigestive system diseasesAmino acidProtein SubunitschemistryDimerizationProtein BindingFEBS letters
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Nouvelles perspectives concernant la structure et la fonction du domaine carboxyl terminal de Hfq

2015

Accumulating evidence indicates that RNA metabolism components assemble into supramolecular cellular structures to mediate functional compartmentalization within the cytoplasmic membrane of the bacterial cell. This cellular compartmentalization could play important roles in the processes of RNA degradation and maturation. These components include Hfq, the RNA chaperone protein, which is involved in the post-transcriptional control of protein synthesis mainly by the virtue of its interactions with several small regulatory ncRNAs (sRNA). The Escherichia coli Hfq is structurally organized into two domains. An N-terminal domain that folds as strongly bent β-sheets within individual protomers to…

IDP intrinsically-disordered proteinslcsh:Lifelcsh:QR1-502sub-membrane macromolecular assemblyPlasma protein bindingsRNA small non-coding RNABiochemistrylcsh:Microbiologyamyloid fibrilsProtein biosynthesis0303 health sciences[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]Escherichia coli Proteins030302 biochemistry & molecular biologyHfqCTRp Hfq C-terminal peptideFTIR Fourier transform infrared spectroscopyNTR N-terminal regionCompartmentalization (psychology)Cell biology[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsRNA Bacterialsmall non-coding ribonucleic acid (RNA)BiochemistryFSD Fourier self-deconvolutionTransfer RNAAmyloid fibrilProtein BindingBiophysicsBiologyHost Factor 1 Protein03 medical and health sciencesEscherichia coliThT thioflavin T[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyProtein Structure QuaternaryncRNA regulatory non-coding RNAPost-transcriptional regulationMolecular Biology030304 developmental biologyOriginal PaperC-terminusRNA[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyCell Biologycellular compartmentalizationWT wild-typeProtein Structure Tertiarylcsh:QH501-531Host Factor 1 ProteinCTR Hfq C-terminal regionribonucleic acid (RNA) processing and degradationBiophysicpost-transcriptional regulationBioscience Reports
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Human Siglec-10 can bind to vascular adhesion protein-1 and serves as its substrate

2009

AbstractLeukocytes migrate from the blood into areas of inflammation by interacting with various adhesion molecules on endothelial cells. Vascular adhesion protein-1 (VAP-1) is a glycoprotein expressed on inflamed endothelium where it plays a dual role: it is both an enzyme that oxidizes primary amines and an adhesin that is involved in leukocyte trafficking to sites of inflammation. Although VAP-1 was identified more than 15 years ago, the counterreceptor(s) for VAP-1 on leukocytes has remained unknown. Here we have identified Siglec-10 as a leukocyte ligand for VAP-1 using phage display screenings. The binding between Siglec-10 and VAP-1 was verified by different adhesion assays, and this…

ImmunologyReceptors Cell SurfaceInflammationCHO CellsPlasma protein bindingBiologyLigandsBiochemistryMice03 medical and health sciencesCricetulus0302 clinical medicinePeptide LibraryVascular BiologyCricetinaeLectinsLeukocyte TraffickingCell AdhesionmedicineAnimalsHumansEndotheliumLymphocytesProtein Structure QuaternaryCell adhesion030304 developmental biologyMice Knockout0303 health sciencesCell adhesion moleculeSoluble cell adhesion moleculesSIGLECCell BiologyHematologyAdhesionrespiratory systembacterial infections and mycosesRecombinant Proteinsrespiratory tract diseasesChemotaxis LeukocyteBiochemistry030220 oncology & carcinogenesisAmine Oxidase (Copper-Containing)medicine.symptomCell Adhesion MoleculesProtein BindingBlood
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Spectroscopic markers of the T-R quaternary transition in human hemoglobin

2004

n questo lavoro, usiamo un protocollo sol-gel per intrappolare e confrontare gli stati quaternari R e T di entrambi i deossigenati (deossiHb) ederivati ​​di ossido di carbonio (HbCO) dell'emoglobina umana. La banda di assorbimento ottico del vicino infrarosso III e lo stretching di CO a infrarossibanda sono utilizzati per rilevare l'effetto della struttura quaternaria sulle proprietà spettrali di deoxyHb e HbCO; confronto con mioglobinaconsente una valutazione dei contributi terziari e quaternari ai turni di banda misurati. La RXLa transizione T è indicata per causare un bluspostamento della banda III di ~ 35 cm?1per deoxyHb e uno spostamento rosso della banda di allungamento CO di soli ~ 0…

InfraredBiophysicsAnalytical chemistryBiochemistryPhase Transitionchemistry.chemical_compoundHemoglobinsSpectroscopy Fourier Transform InfraredHumansFourier transform infrared spectroscopySpectroscopyProtein Structure QuaternaryCarbon MonoxideChemistryOrganic ChemistryNear-infrared spectroscopyBand IIILow temperature spectroscopyTemperatureBand IIICO stretching bandOxygenSol–gel encapsulationCrystallographyKineticsFTIR spectroscopyMyoglobinAbsorption bandProtein quaternary structureBiomarkersProtein Binding
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Small angle neutron scattering study of the quaternary structure of haemocyanin of Rapana thomasiana

1996

Abstract Small angle neutron scattering (SANS) experiments were performed on a series of solutions of haemocyanin (Hc) of Rapana thomasiana . In a first series of solutions, by changing the external contrast a model of the molecule that is apparently in disagreement with electron microscopy (EM) measurements was obtained. The apparent disagreement was resolved by performing experiments on a series of variable protein concentration solutions in D 2 O. The physical parameters of the model, extrapolated to zero concentration, are in excellent agreement with the EM results obtained on samples more dilute than those examined with SANS.

Inorganic ChemistryCrystallographyRapana thomasianaSeries (mathematics)ChemistryOrganic ChemistryAnalytical chemistryMoleculeProtein quaternary structureSmall-angle neutron scatteringProtein concentrationSpectroscopyAnalytical ChemistryJournal of Molecular Structure
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Quaternary and subunit structure of Calliphora arylphorin as deduced from electron microscopy, electrophoresis, and sequence similarities with arthro…

1992

Arylphorin was purified from larvae of the blowfly Calliphora vicina and studied in its oligomeric form and after dissociation at pH 9.6 into native subunits. In accordance with earlier literature, it was electrophoretically shown to be a 500 kDa hexamer (1 x 6) consisting of 78 kDa polypeptides (= subunits). Electron micrographs of negatively stained hexamers show a characteristic curvilinear, equilateral triangle of 12 nm in diameter (top view) and a rectangle measuring 10 x 12 nm (side view). Alternatively, particles in the top view orientation exhibit a roughly circular shape 12 nm in diameter. Crossed immunoelectrophoresis revealed the presence of a major subunit type; the nature of a …

Insectaanimal structuresCalliphora vicinaProtein ConformationPhysiologyStereochemistryProtein subunitmedicine.medical_treatmentMolecular Sequence DataBiologyRandom hexamerBiochemistryCalliphoraEndocrinologyHemolymphmedicineAnimalsAmino Acid SequenceEcology Evolution Behavior and SystematicsGlycoproteinsSequence Homology Amino AcidProtein primary structureSpidersHemocyaninbiology.organism_classificationNephropidaeMicroscopy ElectronBiochemistryInsect HormonesLarvaHemocyaninsInsect ProteinsElectrophoresis Polyacrylamide GelAnimal Science and ZoologyProtein quaternary structureJournal of Comparative Physiology B
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The Mammalian successions of Sicily and Sardinia: a tentative of correlation with the biochronological frame of the Italian peninsula

2009

Islands Stratigraphy Mammals QuaternarySettore GEO/01 - Paleontologia E Paleoecologia
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