Search results for "binding"

showing 10 items of 3896 documents

Small-angle neutron scattering reveals an oxygen-dependent conformational change of the immunogen keyhole limpet hemocyanin type 1 (KLH1).

2001

The respiratory protein of the keyhole limpet, Megathura crenulata, the hemocyanin (KLH), commonly used as an immunogen, binds oxygen cooperatively, which implies the existence of different conformations. For the first time, two different conformations of KLH1 were detected upon oxygenation, a deoxy and an oxy state, using small-angle neutron scattering. Rearrangements in the quaternary structure of KLH1 were predicted from the different radii of gyration and the shifts of the minima and maxima in the scattering curves. Upon oxygenation, KLH1 becomes smaller and more compact. Model reconstruction of KLH1 indicates a hollow cylinder with two rings located close to both ends, which move sligh…

Conformational changeProtein Conformationmedicine.medical_treatmentBiophysicsNeutron scatteringMegathura crenulataBiophysical PhenomenamedicineAnimalsScattering RadiationProtein Structure QuaternaryNeutronsbiologyChemistryScatteringHemocyaninGeneral Medicinebiology.organism_classificationSmall-angle neutron scatteringRespiratory proteinOxygenCrystallographyMolluscaHemocyaninsbiology.proteinKeyhole limpet hemocyaninProtein BindingEuropean biophysics journal : EBJ
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Molecular architecture of a toxin pore: a 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin.

1996

Staphylococcus aureus alpha-toxin is a hydrophilic polypeptide of 293 amino acids that produces heptameric transmembrane pores. During assembly, the formation of a pre-pore precedes membrane permeabilization; the latter is linked to a conformational change in the oligomer. Here, 41 single-cysteine replacement toxin mutants were thiol-specifically labelled with the polarity-sensitive fluorescent probe acrylodan. After oligomerization on membranes, only the mutants with acrylodan attached to residues in the sequence 118-140 exhibited a marked blue shift in the fluorescence emission maximum, indicative of movement of the fluorophore to a hydrophobic environment. Within this region, two functio…

Conformational changeStaphylococcus aureusProtein ConformationMembrane lipidsBacterial ToxinsMolecular Sequence DataBiologyGeneral Biochemistry Genetics and Molecular BiologyCell membraneHemolysin ProteinsProtein structure2-NaphthylaminemedicinePoint MutationAmino Acid SequenceCysteineMolecular BiologyPeptide sequenceFluorescent Dyeschemistry.chemical_classificationBinding SitesGeneral Immunology and MicrobiologyMolecular StructureGeneral NeuroscienceCell MembraneTransmembrane proteinAmino acidmedicine.anatomical_structureMembraneSpectrometry FluorescenceBiochemistrychemistryLiposomesBiophysicsMutagenesis Site-DirectedResearch ArticleThe EMBO journal
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Protofibril formation of amyloid beta-protein at low pH via a non-cooperative elongation mechanism.

2005

Deposition of the amyloid beta-protein (Abeta) in senile or diffuse plaques is a distinctive feature of Alzheimer's disease. The role of Abeta aggregates in the etiology of the disease is still controversial. The formation of linear aggregates, known as amyloid fibrils, has been proposed as the onset and the cause of pathological deposition. Yet, recent findings suggest that a more crucial role is played by prefibrillar oligomeric assemblies of Abeta that are highly toxic in the extracellular environment. In the present work, the mechanism of protofibril formation is studied at pH 3.1, starting from a solution of oligomeric precursors. By combining static light scattering and photon correla…

Conformational changeTime FactorsAmyloidLightNucleationBiophysicsBiochemistryBiophysical PhenomenaDiffusionDynamic light scatteringAlzheimer DiseaseExtracellularHumansScattering RadiationStatic light scatteringMolecular BiologyCoalescence (physics)PhotonsAmyloid beta-PeptidesModels StatisticalDose-Response Relationship DrugChemistryTemperatureCell BiologyHydrogen-Ion ConcentrationModels TheoreticalCrystallographyKineticsSpectrophotometryBiophysicsThermodynamicsElongationPeptidesProtein BindingThe Journal of biological chemistry
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Human Inducible Hsp70: Structures, Dynamics, and Interdomain Communication from All-Atom Molecular Dynamics Simulations

2015

The 70 kDa human heat shock protein is a major molecular chaperone involved in de novo folding of proteins in vivo and refolding of proteins under stress conditions. Hsp70 is related to several "misfolding diseases" and other major pathologies, such as cancer, and is a target for new therapies. Hsp70 is comprised of two main domains: an N-terminal nucleotide binding domain (NBD) and a C-terminal substrate protein binding domain (SBD). The chaperone function of Hsp70 is based on an allosteric mechanism. Binding of ATP in NBD decreases the affinity of the substrate for SBD, and hydrolysis of ATP is promoted by binding of polypeptide segments in the SBD. No complete structure of human Hsp70 is…

Conformational changebiologySaccharomyces cerevisiaeAllosteric regulationPlasma protein bindingbiology.organism_classificationComputer Science ApplicationsMolecular dynamicsBiochemistryCyclic nucleotide-binding domainATP hydrolysisChaperone (protein)biology.proteinBiophysicsPhysical and Theoretical ChemistryJournal of Chemical Theory and Computation
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Evidence for Conformational Mechanism on the Binding of TgMIC4 with β-Galactose-Containing Carbohydrate Ligand

2015

A deeper understanding of the role of sialic/desialylated groups during TgMIC4-glycoproteins interactions has importance to better clarify the odd process of host cell invasion by members of the apicomplexan phylum. Within this context, we evaluated the interaction established by recombinant TgMIC4 (the whole molecule) with sialylated (bovine fetuin) and desialylated (asialofetuin) glycoproteins by using functionalized quartz crystal microbalance with dissipation monitoring (QCM-D). A suitable receptive surface containing recombinant TgMIC4 for monitoring β-galactose-containing carbohydrate ligand (limit of quantification ∼ 40 μM) was designed and used as biomolecular recognition platform t…

Conformational changemedia_common.quotation_subjectCarbohydratesMolecular ConformationProtozoan ProteinsContext (language use)Plasma protein bindingLigandsElectrochemistryGeneral Materials ScienceInternalizationSpectroscopymedia_commonchemistry.chemical_classificationChemistryLigandLECTINASGalactoseSurfaces and InterfacesCondensed Matter PhysicsFetuinBiochemistryQuartz Crystal Microbalance TechniquesAdsorptionTarget proteinGlycoproteinToxoplasmaProtein BindingLangmuir
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Aryl hydrocarbon receptor activation by cAMP vs. dioxin: divergent signaling pathways.

2005

Even before the first vertebrates appeared on our planet, the aryl hydrocarbon receptor ( AHR ) gene was present to carry out one or more critical life functions. The vertebrate AHR then evolved to take on functions of detecting and responding to certain classes of environmental toxicants. These environmental pollutants include polycyclic aromatic hydrocarbons (e.g., benzo[ a ]pyrene), polyhalogenated hydrocarbons, dibenzofurans, and the most potent small-molecular-weight toxicant known, 2,3,7,8-tetrachlorodibenzo- p -dioxin (TCDD or dioxin). After binding of these ligands, the activated AHR translocates rapidly from the cytosol to the nucleus, where it forms a heterodimer with aryl hydroc…

Conservation of Natural ResourcesAryl hydrocarbon receptor nuclear translocatorPolychlorinated DibenzodioxinsTime FactorsTranscription GeneticGenetic VectorsGreen Fluorescent ProteinsImmunoblottingActive Transport Cell NucleusEnvironmentDioxinsLigandschemistry.chemical_compoundMiceCytosolGenes ReporterCell Line TumorCyclic AMPAnimalsImmunoprecipitationReceptorFluorescent Antibody Technique IndirectCell NucleusMultidisciplinarybiologyChemistryColforsinEndogenous mediatorrespiratory systemBiological SciencesAryl hydrocarbon receptorCyclic AMP-Dependent Protein KinasesCytosolProtein TransportBiochemistryBucladesineMicroscopy FluorescenceReceptors Aryl HydrocarbonSecond messenger systembiology.proteinProstaglandinsEnvironmental PollutantsSignal transductionDimerizationToxicantPlasmidsProtein BindingSignal TransductionProceedings of the National Academy of Sciences of the United States of America
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Liver X receptor activation promotes polyunsaturated fatty acid synthesis in macrophages : relevance in the context of atherosclerosis

2015

Objective— Liver X receptors (LXRs) modulate cholesterol and fatty acid homeostasis as well as inflammation. This study aims to decipher the role of LXRs in the regulation of polyunsaturated fatty acid (PUFA) synthesis in macrophages in the context of atherosclerosis. Approach and Results— Transcriptomic analysis in human monocytes and macrophages was used to identify putative LXR target genes among enzymes involved in PUFA biosynthesis. In parallel, the consequences of LXR activation or LXR invalidation on PUFA synthesis and distribution were determined. Finally, we investigated the impact of LXR activation on PUFA metabolism in vivo in apolipoprotein E–deficient mice. mRNA levels of acyl…

Context (language use)Biologydigestive systemchemistry.chemical_compoundMicearachidonic acidAnimalsHumansFatty acid homeostasisReceptorLiver X receptor[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyLiver X Receptorschemistry.chemical_classificationCholesterolFatty acidfood and beveragesArteriesAtherosclerosisOrphan Nuclear ReceptorsmacrophagesBiochemistrychemistryn-3 polyunsaturated fatty acidFatty Acids UnsaturatedArachidonic acidlipids (amino acids peptides and proteins)Cardiology and Cardiovascular MedicineSterol Regulatory Element Binding Protein 1Polyunsaturated fatty acidFoam Cellsliver X receptor
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MicroRNA-Based Therapeutic Perspectives in Myotonic Dystrophy

2019

Myotonic dystrophy involves two types of chronically debilitating rare neuromuscular diseases: type 1 (DM1) and type 2 (DM2). Both share similarities in molecular cause, clinical signs, and symptoms with DM2 patients usually displaying milder phenotypes. It is well documented that key clinical symptoms in DM are associated with a strong mis-regulation of RNA metabolism observed in patient’s cells. This mis-regulation is triggered by two leading DM-linked events: the sequestration of Muscleblind-like proteins (MBNL) and the mis-regulation of the CUGBP RNA-Binding Protein Elav-Like Family Member 1 (CELF1) that cause significant alterations to their important functions in RNA processing. It ha…

Context (language use)miRNA-based drugReviewBioinformaticsMyotonic dystrophyCatalysislcsh:ChemistryInorganic ChemistryMBNL proteinsCELF1microRNADrug DiscoveryMedicineAnimalsHumansPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopyCELF1 ProteinRna processingmyotonic dystrophymicroRNAbusiness.industryOrganic ChemistryAlternative splicingmiRNA-targeting drugRNA-Binding ProteinsGeneral MedicineGenetic Therapymedicine.diseasePhenotypeComputer Science ApplicationsAlternative SplicingMicroRNAslcsh:Biology (General)lcsh:QD1-999Drug developmentGene Expression Regulationantisense oligonucleotidesbusinessFunction (biology)International Journal of Molecular Sciences
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Sorting signals in the cytosolic tail of membrane proteins involved in the interaction with plant ARF1 and coatomer.

2004

Summary In mammals and yeast, a cytosolic dilysine motif is critical for endoplasmic reticulum (ER) localization of type I membrane proteins. Retrograde transport of type I membrane proteins containing dilysine motifs at their cytoplasmic carboxy (C)-terminal tail involves the interaction of these motifs with the COPI coat. The C-terminal dilysine motif has also been shown to confer ER localization to type I membrane proteins in plant cells. Using in vitro binding assays, we have analyzed sorting motifs in the cytosolic tail of membrane proteins, which may be involved in the interaction with components of the COPI coat in plant cells. We show that a dilysine motif in the −3,−4 position (rel…

CooperativityPlant ScienceBiologyCoatomer Proteinchemistry.chemical_compoundGeneticsAmino Acid SequencePlant ProteinsBinding SitesSequence Homology Amino AcidEndoplasmic reticulumProtoplastsMembrane ProteinsOryzaCell BiologyEndoplasmic reticulum localizationCOPIBrefeldin APeptide FragmentsCell biologyKineticsProtein SubunitsMembrane proteinchemistryAmino Acid SubstitutionCoatomerCytoplasmADP-Ribosylation Factor 1Sequence AlignmentSignal TransductionThe Plant journal : for cell and molecular biology
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Strong Cooperativity and Loose Geometry between CUB Domains Are the Basis for Procollagen C-Proteinase Enhancer Activity

2009

Procollagen C-proteinase enhancers (PCPE-1 and -2) specifically activate bone morphogenetic protein-1 (BMP-1) and other members of the tolloid proteinase family during C-terminal processing of fibrillar collagen precursors. PCPEs consist of two CUB domains (CUB1 and CUB2) and one NTR domain separated by one short and one long linker. It was previously shown that PCPEs can strongly interact with procollagen molecules, but the exact mechanism by which they enhance BMP-1 activity remains largely unknown. Here, we used a series of deletion mutants of PCPE-1 and two chimeric constructs with repetitions of the same CUB domain to study the role of each domain and linker. Out of all the forms teste…

CooperativityPlasma protein bindingTransfectionBinding CompetitiveBiochemistryBone morphogenetic protein 1Bone Morphogenetic Protein 1Cell LineHumansAmino Acid SequenceBinding siteEnhancerMolecular BiologyGlycoproteinsExtracellular Matrix ProteinsBinding SitesEnzyme Catalysis and RegulationChemistryCircular DichroismCell BiologyCUB domainKineticsProcollagen peptidaseBiochemistryMutationBiophysicsElectrophoresis Polyacrylamide GelLinkerProcollagenProtein BindingJournal of Biological Chemistry
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