Search results for "protein binding"

showing 10 items of 870 documents

Structural Basis of the High Affinity Interaction between the Alphavirus Nonstructural Protein-3 (nsP3) and the SH3 Domain of Amphiphysin-2

2016

We show that a peptide from Chikungunya virus nsP3 protein spanning residues 1728–1744 binds the amphiphysin-2 (BIN1) Src homology-3 (SH3) domain with an unusually high affinity (Kd 24 nM). Our NMR solution complex structure together with isothermal titration calorimetry data on several related viral and cellular peptide ligands reveal that this exceptional affinity originates from interactions between multiple basic residues in the target peptide and the extensive negatively charged binding surface of amphiphysin-2 SH3. Remarkably, these arginines show no fixed conformation in the complex structure, indicating that a transient or fluctuating polyelectrostatic interaction accounts for this …

0301 basic medicinenuclear magnetic resonance (NMR)Amino Acid MotifsStatic ElectricityPeptideTarget peptidePlasma protein bindingViral Nonstructural ProteinsBiologyhost-pathogen interactionBiochemistrySH3 domainsrc Homology Domainsamphiphysin SH3Structure-Activity Relationship03 medical and health sciencesProtein structuredynaminHumansShort linear motifprotein structureNuclear Magnetic Resonance BiomolecularMolecular BiologySrc homology 3 domain (SH3 domain)Adaptor Proteins Signal Transducingchemistry.chemical_classificationTumor Suppressor Proteinsta1182Nuclear ProteinsIsothermal titration calorimetryCell Biologyintrinsically disordered protein030104 developmental biologychemistryBiochemistrynsP3Protein Structure and FoldingAmphiphysinBiophysicsPeptidesChikungunya virusProtein BindingJournal of Biological Chemistry
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Do genetic polymorphisms in angiotensin converting enzyme 2 (ACE2) gene play a role in coronavirus disease 2019 (COVID-19)?

2020

Abstract Although some demographic, clinical and environmental factors have been associated with a higher risk of developing coronavirus disease 2019 (COVID-19) and progressing towards severe disease, altogether these variables do not completely account for the different clinical presentations observed in patients with comparable baseline risk, whereby some subjects may remain totally asymptomatic, whilst others develop a very aggressive illness. Some predisposing genetic backgrounds can hence potentially explain the broad inter-individual variation of disease susceptibility and/or severity. It has been now clearly established that severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2…

0301 basic medicinereceptorClinical BiochemistryPopulationPneumonia ViralAdipose tissueInflammationPeptidyl-Dipeptidase AAsymptomaticViruspolymorphism03 medical and health sciencesBetacoronavirus0302 clinical medicineProtein DomainsFibrosismedicineHumans030212 general & internal medicineeducationGenePandemicseducation.field_of_studyPolymorphism Geneticbusiness.industrySARS-CoV-2Biochemistry (medical)COVID-19General Medicineangiotensinmedicine.diseaseenzyme030104 developmental biologyCOVID-19 angiotensin enzyme polymorphism receptorImmunologyAngiotensin-converting enzyme 2Spike Glycoprotein CoronavirusReceptors VirusAngiotensin-Converting Enzyme 2medicine.symptombusinessCoronavirus InfectionsProtein Binding
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Hidden complexity in membrane permeabilization behavior of antimicrobial polycations.

2021

A promising alternative to classical antibiotics are antimicrobial peptides and their synthetic mimics (smAMPs) that supposedly act directly on membranes. For a more successful design of smAMPs, we need to know how the type of interaction with the membrane determines the type of membrane perturbation. How this, in turn, transfers into selectivity and microbial killing activity is largely unknown. Here, we characterize the action of two smAMPs: MM:CO (a copolymer of hydrophobic cyclooctyl subunits and charged β-monomethyl-α-aminomethyl subunits) and the highly charged poly-NM (a homopolymer of α-aminomethyl subunits). By thorough characterization of vesicle leakage experiments, we elucidate …

0303 health sciencesMembrane permeabilizationChemistryVesicleKineticsAntimicrobial peptidesStatic ElectricityGeneral Physics and Astronomy010402 general chemistryAntimicrobialFluoresceins01 natural sciencesPermeability0104 chemical sciences03 medical and health sciencesMembraneGlycerophosphatesBiophysicsPhysical and Theoretical ChemistryHydrophobic and Hydrophilic InteractionsUnilamellar Liposomes030304 developmental biologyLeakage (electronics)Antimicrobial Cationic PeptidesProtein BindingPhysical chemistry chemical physics : PCCP
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Physico-chemical study of the radiopharmaceuticals 99mTc-DMSA, 99mTc-EDTA and 99mTc-DTPA interaction with plasmatic proteins.

1989

This report studies the binding rate of the radiopharmaceuticals 99mTc-DTPA, 99mTc-EDTA and 99mTc-DMSA to plasmatic proteins. The proteins bind to the tested radiopharmaceuticals in the following sequence: 99mTc-DTPA less than 99mTc-DMSA(C1) less than 99mTc-EDTA less than 99mTc-DMSA(C2) where C1 and C2 represent two different Tc-DMSA complexes. The thermodynamic study suggests a quantitative relationship of radiopharmaceutical:protein = 1:1 and an almost nonexistent influence of the temperature, which means that the interacting forces in this process are relatively weak.

99mtc dtpaPentetic acid99mTc-DMSAGeneral Engineeringchemistry.chemical_elementTechnetiumPlasma protein bindingBlood ProteinsOrganotechnetium CompoundsPentetic AcidTechnetiumBlood proteinschemistry.chemical_compoundchemistryBiochemistryTechnetium Tc 99m Dimercaptosuccinic AcidTechnetium Tc 99m PentetateEdetic AcidTechnetium Tc 99m Dimercaptosuccinic AcidSulfhydryl CompoundsSuccimerEdetic AcidProtein BindingInternational journal of radiation applications and instrumentation. Part A, Applied radiation and isotopes
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CitA/CitB Two-Component System Regulating Citrate Fermentation in Escherichia coli and Its Relation to the DcuS/DcuR System In Vivo

2011

ABSTRACT Citrate fermentation by Escherichia coli requires the function of the citrate/succinate antiporter CitT ( citT gene) and of citrate lyase ( citCDEFXG genes). Earlier experiments suggested that the two-component system CitA/CitB, consisting of the membrane-bound sensor kinase CitA and the response regulator CitB, stimulates the expression of the genes in the presence of citrate, similarly to CitA/CitB of Klebsiella pneumoniae . In this study, the expression of a chromosomal citC-lacZ gene fusion was shown to depend on CitA/CitB and citrate. CitA/CitB is related to the DcuS/DcuR two-component system which induces the expression of genes for fumarate respiration in response to C 4 -di…

ATP citrate lyaseOperonBiologymedicine.disease_causeMicrobiologyCitric AcidFusion geneGene clusterEscherichia colimedicinePromoter Regions GeneticMolecular BiologyEscherichia coliEscherichia coli ProteinsPromoterGene Expression Regulation BacterialArticlesMolecular biologyTwo-component regulatory systemDNA-Binding ProteinsResponse regulatorBiochemistryFermentationProtein KinasesProtein BindingTranscription FactorsJournal of Bacteriology
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Conversion of the Ca2+-ATPase from Rhodospirillum rubrum into a Mg2+-dependent enzyme by 1,N6-etheno ATP

1980

Nucleoside triphosphate hydrolysis of R.rubrum ATPase complexes can be changed from Ca2+-dependence to Mg2+-dependence by replacing ATP with 1,N6-etheno ATP. Four ATPase complexes which have been prepared by different procedures hydrolyze ATP and 1,N6-etheno ATP at different rates in dependence on the added metal ions. These differences allow an easy distinction of the various enzyme forms.

ATPaseBiophysicsPhotophosphorylationCalcium-Transporting ATPasesRhodospirillum rubrumBiochemistrychemistry.chemical_compoundAdenosine TriphosphateMagnesiumMolecular BiologyEdetic Acidchemistry.chemical_classificationbiologyATP synthaseChemiosmosisCell MembraneRhodospirillum rubrumCell Biologybiology.organism_classificationKineticsEnzymeBiochemistrychemistrybiology.proteinNucleoside triphosphateOligomycinsATP synthase alpha/beta subunitsEthenoadenosine TriphosphateProtein BindingBiochemical and Biophysical Research Communications
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Structural and Dynamic Properties of the Homodimeric Hemoglobin from Scapharca inaequivalvis Thr-72→Ile Mutant: Molecular Dynamics Simulation, Low Te…

1998

AbstractMolecular dynamics simulations, low temperature visible absorption spectroscopy, and resonance Raman spectroscopy have been performed on a mutant of the Scapharca inaequivalvis homodimeric hemoglobin, where residue threonine 72, at the subunit interface, has been substituted by isoleucine. Molecular dynamics simulation indicates that in the Thr-72→Ile mutant several residues that have been shown to play a role in ligand binding fluctuate around orientations and distances similar to those observed in the x-ray structure of the CO derivative of the native hemoglobin, although the overall structure remains in the T state. Visible absorption spectroscopy data indicate that in the deoxy …

Absorption spectroscopyProtein subunitDimerResonance Raman spectroscopyMutantBiophysicsHemeSpectrum Analysis Ramanchemistry.chemical_compoundHemoglobinsMutant proteinAnimalsHemeHistidineCarbon MonoxideChemistrySettore BIO/11TemperatureWaterCrystallographyMolluscaSpectrophotometryMutationDimerizationProtein BindingResearch ArticleBiophysical Journal
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Binding of a fluorescent dansylcadaverine-substance P analogue to negatively charged phospholipid membranes.

2000

Abstract We have investigated the binding of a new dansylcadaverine derivative of substance P (DNC-SP) with negatively charged small unilamellar vesicles composed of a mixture of phosphatidylcholine (PC) and either phosphatidylglycerol (PG) or phosphatidylserine (PS) using fluorescence spectroscopic techniques. The changes in fluorescence properties were used to obtain association isotherms at variable membrane negative charges and at different ionic strengths. The experimental association isotherms were analyzed using two binding approaches: (i) the Langmuir adsorption isotherm and the partition equilibrium model, that neglect the activity coefficients; and (ii) the partition equilibrium m…

Activity coefficientVesicleLipid BilayersAnalytical chemistryLangmuir adsorption modelCharge densityGeneral MedicineSubstance PBiochemistryBinding constantFluorescencechemistry.chemical_compoundsymbols.namesakeMembranechemistryModels ChemicalStructural BiologyPhosphatidylcholinePartition equilibriumCadaverinesymbolsMolecular BiologyPhospholipidsFluorescent DyesProtein BindingInternational journal of biological macromolecules
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Genome-wide characterization of chromatin binding and nucleosome spacing activity of the nucleosome remodelling ATPase ISWI.

2010

The evolutionarily conserved ATP-dependent nucleosome remodelling factor ISWI can space nucleosomes affecting a variety of nuclear processes. In Drosophila, loss of ISWI leads to global transcriptional defects and to dramatic alterations in higher-order chromatin structure, especially on the male X chromosome. In order to understand if chromatin condensation and gene expression defects, observed in ISWI mutants, are directly correlated with ISWI nucleosome spacing activity, we conducted a genome-wide survey of ISWI binding and nucleosome positioning in wild-type and ISWI mutant chromatin. Our analysis revealed that ISWI binds both genic and intergenic regions. Remarkably, we found that ISWI…

Adenosine TriphosphatasesMaleChromatin ImmunoprecipitationX ChromosomeD. melanogasterSettore INF/01 - Informaticachromatin remodellingGenomicsChromatin Assembly and DisassemblyArticleNucleosomesDNA-Binding ProteinsISWInucleosome spacingGene Expression RegulationSettore BIO/10 - BiochimicaAnimalsDrosophila ProteinsDrosophilaPromoter Regions GeneticCrosses GeneticProtein BindingTranscription FactorsThe EMBO journal
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Nested MWC model describes hydrolysis of GroEL without assuming negative cooperativity in binding

2002

Folding assistance and ATPase activity of GroEL are based on the existence of different conformations. In order to characterise these conformations, published data on steady state ATPase activity in the absence of GroES were reanalysed simultaneously in terms of the Nested MWC model. This model is a hierarchical extension of the symmetry-model of Monod et al. [J. Mol. Biol. 12 (1965) 88]. An unique set of GroEL specific parameters was obtained. This set was supported by comparison of predictions arising from this set of values with experimental data for hydrolysis of ATP in the presence of ADP and ATPgammaS, binding of ATPgammaS and ADP to GroEL in the absence of ATP, and binding of ATP as …

Adenosine TriphosphatasesModels Molecularchemistry.chemical_classificationChemistryHydrolysisBiophysicsCooperative bindingCooperativityChaperonin 60GroESBiochemistryGroELAnalytical ChemistryAdenosine DiphosphateFolding (chemistry)CrystallographyAdenosine TriphosphateATP hydrolysisCalibrationBiophysicsComputer SimulationNucleotideSteady state (chemistry)Molecular BiologyProtein BindingBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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