Search results for "binding sites"

showing 10 items of 636 documents

Carbohydrate binding specificity and purification by biospecific affinity chromatography of Ascidiamalaca traust. Hemagglutinins

1982

The carbohydrate specificities of Ascidia malaca serum hemagglutinins were determined by hemagglutination inhibition tests. Analysis of agglutinins against rabbit and human A, B, O erythrocytes suggests that the size of the combining site corresponds to a disaccharide with a specificity for saccharides containing a D-galacto configuration (D-melibiose, D-raffinose, D-galactose, alpha-lactose, lactulose, L-arabinose). No anomeric specificity was observed with oligosaccharides. Hydroxyl groups probably involved in hydrogen-bond formation with agglutinin binding site, were identified as carbons C2, C4, C5 and C6 of D-galactose. Absorption experiments showed that two distinct agglutinins with s…

Hemagglutination Inhibition TestsErythrocytesImmunologyDisaccharideBiologyChromatography Affinitychemistry.chemical_compoundRaffinoseAgglutininSpecies SpecificityAffinity chromatographyAnimalsHumansUrochordataBinding sitePolyacrylamide gel electrophoresisBinding selectivityMelibioseBinding SitesGalactoseHemagglutination TestsHemagglutination Inhibition TestsAgglutination (biology)HemagglutininschemistryBiochemistryAntibody FormationCarbohydrate MetabolismRabbitsDevelopmental BiologyDevelopmental & Comparative Immunology
researchProduct

Cyanide binding and heme cavity conformational transitions in **Drosophila melanogaster** hexacoordinate hemoglobin

2006

The reason for the presence of hemoglobin-like molecules in insects, such as Drosophila melanogaster, that live in fully aerobic environments has yet to be determined. Heme endogenous hexacoordination (where HisE7 and HisF8 axial ligands to the heme Fe atom are both provided by the protein) is a recently discovered mechanism proposed to modulate O-2 affinity in hemoglobins from different species. Previous results have shown that D. melanogaster hemoglobin 1 (product of the glob1 gene) displays heme endogenous hexacoordination in both the ferrous and ferric states. Here we present kinetic data characterizing the exogenous cyanide ligand binding process, and the three-dimensional structure (a…

HemeproteinStereochemistryProtein ConformationCyanideMolecular Sequence DataNeuroglobinNerve Tissue ProteinsHemeCrystallography X-RayLigandsBiochemistrychemistry.chemical_compoundHemoglobinsMiceSequence Analysis ProteinMelanogasterAnimalsDrosophila ProteinsHumansCRYSTAL-STRUCTUREHistidineHemeBinding SitesCyanidesbiologyCytoglobinCytoglobinHexacoordinatebiology.organism_classificationGlobinsFERRIC APLYSIAKineticsDrosophila melanogasterchemistryHUMAN NEUROGLOBINAPLYSIA-LIMACINA MYOGLOBINX-RAYHemoglobinDrosophila melanogaster
researchProduct

Hepatitis B core particles as a universal display model: a structure-function basis for development

1999

AbstractBecause it exhibits a remarkable capability to accept mutational intervention and undergo correct folding and self-assembly in all viable prokaryotic and eukaryotic expression systems, hepatitis B core (HBc) protein has been favored over other proposed particulate carriers. Structurally, the unusual α-helical organization of HBc dimeric units allows introduction of foreign peptide sequences into several areas of HBc shells, including their most protruding spikes. Progress toward full resolution of the spatial structure as well as accumulation of chimeric HBc-based structures has brought closer the knowledge-based design of future vaccines, gene therapy tools and other artificial par…

Hepatitis B virusGenes ViralCryo-electron microscopyMacromolecular SubstancesProtein ConformationBiophysicsComputational biologyBiologyBiochemistryMolecular displayEpitopesProtein structureStructural BiologyGeneticsProkaryotic expressionAnimalsHumansMolecular BiologyDrug CarriersBinding SitesSpatial structureViral Core ProteinsStructure functionHepatitis B core proteinvirus diseasesCell BiologyBasis (universal algebra)Self-assemblyAntigenicityVirologyBiological EvolutionHepatitis B Core Antigensdigestive system diseasesFolding (chemistry)Protein structureElectron cryomicroscopyDimerizationHepatitis b coreFEBS Letters
researchProduct

N-terminal myristoylation-dependent masking of neutralizing epitopes in the preS1 attachment site of hepatitis B virus

2011

The N-terminally myristoylated preS1 domain of the large hepatitis B surface protein (LHBs) mediates specific attachment of hepatitis B virus (HBV) to hepatocytes. Its B-cell epitopes leading to neutralization of infectivity are not yet characterized.We inserted C- and N-terminal preS1 peptides into the most immunogenic region of HBV core particles, therewith immunized Balb/c mice and determined binding properties and neutralization potential of resulting antibodies in vitro.The particles with preS1 inserts were highly immunogenic and the corresponding anti-preS antibodies strongly bound to HBV particles from chronic carriers infected with different HBV genotypes A-F. However, antibodies bi…

Hepatitis B virusHBsAgGenotypeMolecular Sequence DataIn Vitro TechniquesBiologymedicine.disease_causeMyristic AcidNeutralizationEpitopeMice03 medical and health sciencesHepatitis B Chronic0302 clinical medicinemedicineAnimalsHumansHepatitis B VaccinesAmino Acid SequenceHepatitis B AntibodiesProtein Precursors030304 developmental biologyHepatitis B virusInfectivityMice Inbred BALB C0303 health sciencesBinding SitesHepatitis B Surface AntigensSequence Homology Amino AcidHepatologyHepatitis Bmedicine.diseaseAntibodies NeutralizingVirology3. Good healthEpitope mappingbiology.proteinEpitopes B-Lymphocyte030211 gastroenterology & hepatologyAntibodyEpitope MappingJournal of Hepatology
researchProduct

Sequence-Specific Repression of Cotranslational Translocation of the Hepatitis B Virus Envelope Proteins Coincides with Binding of Heat Shock Protein…

1997

AbstractThe large L envelope protein of the hepatitis B virus has the peculiar capacity to adopt two transmembrane topologies. The N-terminal preS domain of L initially remains in the cytosol while the S domain is cotranslationally inserted into the endoplasmic reticulum membrane. The preS region of about half of the L molecules is posttranslationally translocated to the lumenal space. We now demonstrate that the repression of cotranslational translocation of preS is conferred by a preS1-specific sequence. By analysis of L deletion mutants, the cytosolic anchorage determinant was mapped to amino acid sequence 70 to 94 of L. The intrinsic potential of this determinant to suppress cotranslati…

Hepatitis B virusHSC70 Heat-Shock ProteinsRecombinant Fusion ProteinsPlasma protein bindingBiologyGenes envCytosolViral Envelope ProteinsHeat shock proteinVirologyHumansHSP70 Heat-Shock ProteinsBinding sitePromoter Regions GeneticPeptide sequenceBinding SitesBase SequenceCell-Free SystemEndoplasmic reticulumHSC70 Heat-Shock ProteinsOligonucleotides AntisenseMolecular biologyTransmembrane proteinChaperone (protein)Protein Biosynthesisbiology.proteinMutagenesis Site-DirectedMetallothioneinCarrier ProteinsProtein BindingVirology
researchProduct

Priming of cytotoxic T cell responses to exogenous hepatitis B virus core antigen is B cell dependent

2003

The hepatitis B virus (HBV) core antigen (HBcAg) has a unique ability to bind a high frequency of naive human and murine B cells. The role of HBcAg-binding naive B cells in the immunogenicity of HBcAg is not clear. The HBcAg-binding properties of naive B cells were characterized using HBcAg particles with mutated spike region (residues 76-85) sequences. Deletion of residues 76-85 (HBcDelta76-85) destroyed naive B cell binding, whereas deletion of residues 79-85 did not. HBcAg particles with an Ile instead of the natural Ala at position 80 did not bind naive B cells, whereas reversion of Ile80--Ala restored B cell binding. Destroying the B cell-binding ability of HBcAg had a marginal effect …

Hepatitis B virusMolecular Sequence DataNaive B cellPriming (immunology)Biologymedicine.disease_causeMiceAntigenVirologymedicineAnimalsCytotoxic T cellHepatitis B VaccinesAmino Acid SequenceHepatitis B AntibodiesB cellHepatitis B virusB-LymphocytesVaccines SyntheticBinding SitesImmunogenicityVirionvirus diseasesHepatitis BHepatitis B Core AntigensVirologyRecombinant Proteinsdigestive system diseasesMice Inbred C57BLHBcAgmedicine.anatomical_structureImmunizationT-Lymphocytes Cytotoxic
researchProduct

Hepatitis B Virus Large Envelope Protein Interacts with γ2-Adaptin, a Clathrin Adaptor-Related Protein

2001

ABSTRACT For the outcome of a hepatitis B virus (HBV) infection, the viral L envelope protein with its pre-S domain performs pivotal functions by mediating attachment of HBV to liver cells, envelopment of viral capsids, release of (sub)viral particles, regulation of supercoiled DNA amplification, and transcriptional transactivation. To assess its multiple functions and host-protein assistance involved, we initiated a two-hybrid screen using the L-specific pre-S1 domain as bait. With this approach, we have identified γ2-adaptin, a putative member of the clathrin adaptor proteins responsible for protein sorting and trafficking, as a specific binding partner of L protein. Evidence for a physic…

Hepatitis B virusVesicle-associated membrane protein 8ImmunoprecipitationImmunologyGolgi ApparatusTransfectionmedicine.disease_causeMicrobiologyClathrinChromatography AffinityCytosolViral Envelope ProteinsMutant proteinYeastsVirologyProtein targetingmedicineAnimalsBinding siteAdaptor Protein Complex gamma SubunitsBinding SitesbiologyMembrane ProteinsPrecipitin TestsClathrinTransmembrane proteinVirus-Cell InteractionsCell biologyInsect ScienceCOS CellsMutationbiology.proteinClathrin adaptor proteinsProtein BindingJournal of Virology
researchProduct

The binding of intravenous and oral biliary contrast agents to human and bovine serum albumin

1978

The binding of two homologous series of oral and intravenous biliary contrast agents to human and bovine serum albumin was investigated using the gel filtration technique. All intravenous compounds are bound to human serum albumin via one high affinity and several low affinity binding sites. Within the concentration range investigated, about 3--5 high affinity binding sites for the oral compounds were found on human serum albumin. In general, the intravenous compounds have a greater affinity for human serum albumin than the oral compounds. No significant differences were found for the binding of the oral compounds to human or bovine serum albumin, while the intravenous compounds have a high…

High affinity bindingSize-exclusion chromatographySerum albuminAdministration OralContrast MediaPlasma protein bindingIn Vitro TechniquesPharmacologyLow affinitymedicineAnimalsHumansBovine serum albuminBinding siteBiliary TractSerum AlbuminPharmacologyBinding SitesbiologyChemistrySerum Albumin BovineGeneral MedicineHydrogen-Ion ConcentrationHuman serum albuminRadiographySolubilityBiochemistryInjections Intravenousbiology.proteinCattleProtein Bindingmedicine.drugNaunyn-Schmiedeberg's Archives of Pharmacology
researchProduct

Mapping the cell binding site on high molecular weight kininogen domain 5.

1995

Investigations mapped the region(s) on the light chain of high molecular weight kininogen (HK) that participates in cell binding. Sequential and overlapping peptides of domain 5 (D5H) were synthesized to determine its cell binding site(s). Three peptides from non-overlapping regions on D5H were found to inhibit biotin-HK binding to endothelial cells. Peptides GKE19 and HNL 21 weakly inhibited biotin-HK binding with IC50 of 792 and 215 microM, respectively. Peptide HKH20 inhibited biotin-HK binding with an IC50 of 0.2 microM. Two peptides, GGH18 and HVL24, which overlapped HKH20, also inhibited biotin-HK binding to endothelial cells with IC50 values of 108 and 0.8 microM, respectively. Bioti…

High-molecular-weight kininogenMolecular Sequence DataBiotinPeptideBiochemistryHumansAmino Acid SequenceBinding siteMolecular BiologyCells Culturedchemistry.chemical_classificationKininogenBinding SitesbiologyCoagulantsKininogensCell BiologyMolecular biologyPeptide FragmentsMolecular WeightEnzymechemistryPolyclonal antibodiesBiotinylationbiology.proteinEndothelium VascularAntibodyProtein BindingThe Journal of biological chemistry
researchProduct

Distribution patterns of neoglycoprotein-binding sites (endogenous lectins) and lectin-reactive glycoconjugates during cartilage and bone formation i…

1995

The distribution of endogenous lectins, visualized by labelled neoglycoproteins, and of defined oligosaccharide structures, reactive with plant lectins, during fetal development of the fingers was analyzed in sections of human 3- to 8-month-old fetal specimens. Chondrogenesis as well as ossification were correlated with characteristic modulations in the expression of both glycoligand-binding molecules and characteristic carbohydrate structures. Occurrence of xylose-specific receptors was judged to be an early sign of cartilage development. Similarly, α-mannosyl residues that had been attached to labelled carrier proteins were strongly bound by the extracellular matrix already during early s…

HistologyCartilage metabolismBone tissueFingersExtracellular matrixPregnancyLectinsmedicineHumansGlycoproteinsBinding SitesBone DevelopmentbiologyHistocytochemistryChemistryOssificationOsteoidCartilageLectinChondrogenesisCartilagemedicine.anatomical_structureBiochemistrybiology.proteinFemaleAnatomymedicine.symptomGlycoconjugates
researchProduct