Search results for "DAS"

showing 10 items of 4164 documents

Flavonoids as noncompetitive inhibitors of Dengue virus NS2B-NS3 protease: Inhibition kinetics and docking studies

2014

NS2B-NS3 is a serine protease of the Dengue virus considered a key target in the search for new antiviral drugs. In this study flavonoids were found to be inhibitors of NS2B-NS3 proteases of the Dengue virus serotypes 2 and 3 with IC50 values ranging from 15 to 44 μM. Agathisflavone (1) and myricetin (4) turned out to be noncompetitive inhibitors of dengue virus serotype 2 NS2B-NS3 protease with Ki values of 11 and 4.7 μM, respectively. Docking studies propose a binding mode of the flavonoids in a specific allosteric binding site of the enzyme. Analysis of biomolecular interactions of quercetin (5) with NT647-NHS-labeled Dengue virus serotype 3 NS2B-NS3 protease by microscale thermophoresis…

Models MolecularProteasesSerine Proteinase Inhibitorsvirusesmedicine.medical_treatmentClinical BiochemistryPharmaceutical ScienceDengue virusmedicine.disease_causeAntiviral AgentsBiochemistryStructure-Activity Relationshipchemistry.chemical_compoundDrug DiscoverymedicineMolecular BiologyFlavonoidsSerine proteaseNS3ProteasebiologyMicroscale thermophoresisSerine EndopeptidasesOrganic ChemistryDengue VirusVirologyMolecular Docking SimulationKineticschemistryBiochemistryDocking (molecular)biology.proteinMolecular MedicineMyricetinBioorganic & Medicinal Chemistry
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Evidence for substrate binding-induced zwitterion formation in the catalytic Cys-His dyad of the SARS-CoV main protease.

2014

The coronavirus main protease (M(pro)) represents an attractive drug target for antiviral therapy of coronavirus (CoV) infections, including severe acute respiratory syndrome (SARS). The SARS-CoV M(pro) and related CoV proteases have several distinct features, such as an uncharged Cys-His catalytic dyad embedded in a chymotrypsin-like protease fold, that clearly separate these enzymes from archetypical cysteine proteases. To further characterize the catalytic system of CoV main proteases and to obtain information about improved inhibitors, we performed comprehensive simulations of the proton-transfer reactions in the SARS-CoV M(pro) active site that lead to the Cys(-)/His(+) zwitterionic st…

Models MolecularProteasesStereochemistryvirusesmedicine.medical_treatmentEntropyStatic ElectricityMolecular Dynamics Simulationmedicine.disease_causeBiochemistrySubstrate Specificitychemistry.chemical_compoundViral ProteinsCatalytic DomainmedicineHistidineCysteineHistidineCoronavirus 3C ProteasesCoronaviruschemistry.chemical_classificationProteasebiologyChemistryvirus diseasesActive siteCysteine EndopeptidasesEnzymeBiochemistryZwitterionbiology.proteinCysteineBiochemistry
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Effects of ligand binding on the mechanical properties of ankyrin repeat protein gankyrin.

2012

Ankyrin repeat proteins are elastic materials that unfold and refold sequentially, repeat by repeat, under force. Herein we use atomistic molecular dynamics to compare the mechanical properties of the 7-ankyrin-repeat oncoprotein Gankyrin in isolation and in complex with its binding partner S6-C. We show that the bound S6-C greatly increases the resistance of Gankyrin to mechanical stress. The effect is specific to those repeats of Gankyrin directly in contact with S6-C, and the mechanical ‘hot spots’ of the interaction map to the same repeats as the thermodynamic hot spots. A consequence of stepwise nature of unfolding and the localized nature of ligand binding is that it impacts on all as…

Models MolecularProteasome Endopeptidase ComplexGankyrinBiophysicsPlasma protein bindingMolecular Dynamics SimulationLigands01 natural sciencesProtein–protein interaction03 medical and health sciencesCellular and Molecular NeuroscienceMolecular dynamicsProto-Oncogene Proteins0103 physical sciencesGeneticsProteasome endopeptidase complexBiologyMolecular Biologylcsh:QH301-705.5Ecology Evolution Behavior and Systematics030304 developmental biology0303 health sciences010304 chemical physicsEcologybiologyChemistryComputational BiologyAnkyrin Repeat ProteinMolecular biologyComputational Theory and Mathematicslcsh:Biology (General)Modeling and Simulationigand Binding Mechanical Properties Ankyrin Repeat Proteinbiology.proteinBiophysicsAnkyrin repeatStress MechanicalProtein BindingResearch ArticleMacromoleculePLoS Computational Biology
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Antigen processing influences HIV-specific cytotoxic T lymphocyte immunodominance

2016

Udgivelsesdato: 2009-May-03 Although cytotoxic T lymphocytes (CTLs) in people infected with human immunodeficiency virus type 1 can potentially target multiple virus epitopes, the same few are recognized repeatedly. We show here that CTL immunodominance in regions of the human immunodeficiency virus type 1 group-associated antigen proteins p17 and p24 correlated with epitope abundance, which was strongly influenced by proteasomal digestion profiles, affinity for the transporter protein TAP, and trimming mediated by the endoplasmatic reticulum aminopeptidase ERAAP, and was moderately influenced by HLA affinity. Structural and functional analyses demonstrated that proteasomal cleavage 'prefer…

Models MolecularProteasome Endopeptidase ComplexHIV AntigensMolecular Sequence DataImmunologyAntigen presentationHIV Core Protein p24HIV InfectionsImmunodominanceMajor histocompatibility complexgag Gene Products Human Immunodeficiency VirusEpitopeEvolution MolecularMajor Histocompatibility ComplexLeucyl Aminopeptidase03 medical and health sciences0302 clinical medicineAntigenHumansImmunology and AllergyCytotoxic T cellAmino Acid Sequence030304 developmental biologyAntigen Presentation0303 health sciencesHLA-A AntigensbiologyImmunodominant EpitopesAntigen processingVirology3. Good healthCTL*MutationHIV-1biology.proteinATP-Binding Cassette TransportersProtein BindingT-Lymphocytes Cytotoxic030215 immunologyRETROVIROLOGY
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Synthesis and Inhibitory Studies of Phosphonic Acid Analogues of Homophenylalanine and Phenylalanine towards Alanyl Aminopeptidases.

2020

A library of novel phosphonic acid analogues of homophenylalanine and phenylalanine, containing fluorine and bromine atoms in the phenyl ring, have been synthesized. Their inhibitory properties against two important alanine aminopeptidases, of human (hAPN, CD13) and porcine (pAPN) origin, were evaluated. Enzymatic studies and comparison with literature data indicated the higher inhibitory potential of the homophenylalanine over phenylalanine derivatives towards both enzymes. Their inhibition constants were in the submicromolar range for hAPN and the micromolar range for pAPN, with 1-amino-3-(3-fluorophenyl) propylphosphonic acid (compound 15c) being one of the best low-molecular inhibitors …

Models MolecularProtein Conformation alpha-HelicalMolecular modelStereochemistryPhosphorous AcidsSwinePhenylalaninelcsh:QR1-502PhenylalanineCD13 Antigenscomputer-aided simulationsInhibitory postsynaptic potential01 natural sciencesBiochemistrylcsh:MicrobiologyArticlePhenylalanine derivativesSubstrate SpecificitySmall Molecule Libraries03 medical and health sciencesStructure-Activity RelationshipAnimalsHumansProtein Interaction Domains and MotifsEnzyme Inhibitorsphosphonic acid inhibitorsMolecular Biology030304 developmental biologyAlaninechemistry.chemical_classification0303 health sciencesInhibitory potentialBinding Sites010405 organic chemistryChemistryAminobutyratesFluorineBromine0104 chemical sciencesIsoenzymesKineticsEnzymehuman and porcine alanine aminopeptidasefluorine and bromine substitutionThermodynamicsProtein Conformation beta-StrandProtein BindingBiomolecules
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Mass Spectrometry and Structural Biology Techniques in the Studies on the Coronavirus-Receptor Interaction

2020

Mass spectrometry and some other biophysical methods, have made substantial contributions to the studies on severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and human proteins interactions. The most interesting feature of SARS-CoV-2 seems to be the structure of its spike (S) protein and its interaction with the human cell receptor. Mass spectrometry of spike S protein revealed how the glycoforms are distributed across the S protein surface. X-ray crystallography and cryo-electron microscopy made huge impact on the studies on the S protein and ACE2 receptor protein interaction, by elucidating the three-dimensional structures of these proteins and their conformational changes. The…

Models MolecularProtein Conformation alpha-HelicalvirusesGene ExpressionPharmaceutical ScienceReviewPlasma protein bindingSevere Acute Respiratory Syndromemedicine.disease_causeAnalytical Chemistry0302 clinical medicineDrug Discovery030212 general & internal medicineReceptorPeptide sequenceCoronavirus0303 health sciencesChemistrySevere acute respiratory syndrome-related coronavirusBiochemistryChemistry (miscellaneous)Host-Pathogen InteractionsSpike Glycoprotein CoronavirusReceptors VirusMolecular MedicineAngiotensin-Converting Enzyme 2Coronavirus InfectionsProtein BindingglycosylationSARS coronavirusPneumonia Viralstructural techniquesSequence alignmentPeptidyl-Dipeptidase AMass spectrometrylcsh:QD241-441Betacoronavirus03 medical and health scienceslcsh:Organic chemistryspike protein-ACE2 interactionmedicineHumansProtein Interaction Domains and MotifsAmino Acid SequencePhysical and Theoretical ChemistryBinding sitePandemics030304 developmental biologyBinding SitesSARS-CoV-2Organic ChemistryCOVID-19MSStructural biologyProtein Conformation beta-StrandSequence AlignmentMolecules
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Concentration dependent effects of commonly used pesticides on activation versus inhibition of the quince (Cydonia Oblonga) polyphenol oxidase

2009

Polyphenol oxidase (PPO) catalyzes the oxidation of o-diphenols to their respective quinones which undergo autopolymerization and form dark pigments. The interaction of PPO with various substrates and effectors remains the focus of intensive investigations due to the enzyme's key role in pigments biosynthesis including animal melanogenesis and fruit/fungi enzymatic browning. In this study, the effect of a range of commonly used pesticides on the enzyme activity has been evaluated using the purified quince (Cydonia oblonga Miller) PPO. The biochemical analysis showed that, in the presence of high pesticide concentrations, the enzyme was competitively inhibited, particularly with benomyl, car…

Models MolecularProtein ConformationMolecular Sequence DataCrystallography X-RayToxicologyPolyphenol oxidasechemistry.chemical_compoundCarbarylParathion methylAmino Acid SequenceEnzyme InhibitorsIpomoea batatasPesticidesCatechol oxidaseRosaceaeDose-Response Relationship DrugbiologyReverse Transcriptase Polymerase Chain ReactionComputational BiologyGeneral MedicineNucleic acid amplification techniqueEnzyme assayEnzyme ActivationKineticsParathionchemistryBiochemistryPolyphenolFruitbiology.proteinElectrophoresis Polyacrylamide GelNucleic Acid Amplification TechniquesCatechol OxidaseFood ScienceFood and Chemical Toxicology
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Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane.

2012

Ectodomain shedding at the cell surface is a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane. Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression. In addition, it cleaves amyloid precursor protein (APP) at the β-secretase site, giving rise to amyloidogenic peptides. We have solved the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase…

Models MolecularProtein ConformationPlasma protein bindingCell membrane03 medical and health sciencesProtein structureZymogenAmyloid precursor proteinmedicineHumans030304 developmental biology0303 health sciencesMultidisciplinaryCrystallographybiologyChemistry030302 biochemistry & molecular biologyCell MembraneMetalloendopeptidasesSheddaseBiological SciencesTransmembrane protein3. Good healthCell biologyProtein Structure Tertiarymedicine.anatomical_structureBiochemistryEctodomainbiology.proteinDimerizationProtein BindingProceedings of the National Academy of Sciences of the United States of America
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Jararhagin-derived RKKH Peptides Induce Structural Changes in α1I Domain of Human Integrin α1β1

2003

Integrin alpha(1)beta(1) is one of four collagen-binding integrins in humans. Collagens bind to the alphaI domain and in the case of alpha(2)I collagen binding is competitively inhibited by peptides containing the RKKH sequence and derived from the metalloproteinase jararhagin of snake venom from Bothrops jararaca. In alpha(2)I, these peptides bind near the metal ion-dependent adhesion site (MIDAS), where a collagen (I)-like peptide is known to bind; magnesium is required for binding. Published structures of the ligand-bound "open" conformation of alpha(2)I differs significantly from the "closed" conformation seen in the structure of apo-alpha(2)I near MIDAS. Here we show that two peptides,…

Models MolecularProtein ConformationStereochemistryIntegrinAlpha (ethology)PeptideCrystallography X-RayBinding CompetitiveBiochemistryCollagen Type IProtein Structure SecondaryIntegrin alpha1beta1Protein structureCrotalid VenomsHumansMagnesiumAmino Acid SequenceBinding siteMolecular BiologyPeptide sequenceFluorescent Dyeschemistry.chemical_classificationBinding SitesCalorimetry Differential ScanningMolecular StructurebiologyMetalloendopeptidasesCell BiologyPeptide FragmentsRecombinant ProteinsSpectrometry FluorescencechemistryJararhaginHelixbiology.proteinCrystallizationJournal of Biological Chemistry
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Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism

2000

The enzymes tyrosinase, catecholoxidase and hemocyanin all share similar active sites, although their physiological functions differ. Hemocyanins serve as oxygen carrier proteins, and tyrosinases and catecholoxidases (commonly referred to as phenoloxidases in arthropods) catalyze the hydroxylation of monophenols or the oxidation of o-diphenols to o-quinones, or both. Tyrosinases are activated in vivo by limited proteolytic cleavage, which might open up substrate access to the catalytic site. It has recently been demonstrated that if hemocyanins are subjected to similar proteolytic treatments (in vitro) they also exhibit at least catecholoxidase reactivity. On the basis of their molecular st…

Models MolecularProtein ConformationTyrosinasemedicine.medical_treatmentchemical and pharmacologic phenomenaBiochemistrySubstrate SpecificityHydroxylationchemistry.chemical_compoundProtein structuremedicineAnimalsBinding siteCatechol oxidaseMolecular Biologychemistry.chemical_classificationBinding SitesMolecular StructurebiologyMonophenol MonooxygenaseHemocyaninEnzyme ActivationEnzymechemistryBiochemistryStructural biologyHemocyaninsbiology.proteinCatechol OxidaseTrends in Biochemical Sciences
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