Search results for "binding site"

showing 10 items of 856 documents

Structure of rat odorant-binding protein OBP1 at 1.6 angstrom resolution

2009

The nasal mucosa is a specialist interfacial region sandwiched between the olfactory system and the gaseous chemical milieu. In mammals and insects, this region is rich in odorant-binding proteins that are thought to aid olfaction by assisting mass transfer of the many different organoleptic compounds that make up the olfactory landscape. However, in mammals at least, our grasp on the exact function of odorant-binding proteins is tentative and better insight into the role of these proteins is warranted, not least because of their apparent significance in the olfactory systems of insects. Here, the crystal structure of rat odorant-binding protein 1 is reported at 1.6 Å resolution. This prote…

Models MolecularOlfactory systemCristallographyProtein ConformationRecombinant Fusion ProteinsMolecular Sequence DataOlfactionOBP1Crystallography X-RayReceptors Odorant010402 general chemistry01 natural sciencesPheromonesPichia pastoris03 medical and health sciences[ CHIM.CRIS ] Chemical Sciences/CristallographyProtein structureSpecies SpecificityStructural BiologyODORANT-BINDING PROTEINS[CHIM.CRIS]Chemical Sciences/CristallographyAnimalsAmino Acid SequencePeptide sequence030304 developmental biology0303 health sciencesBinding SitesSequence Homology Amino AcidbiologyProteinsGeneral MedicineLigand (biochemistry)biology.organism_classificationLipocalinsRatsCristallographie0104 chemical sciencesTransport proteinDNA-Binding ProteinsBiochemistryOdorant-binding proteinbiology.proteinODORANT-BINDING PROTEINS;OBP1Sequence Alignment
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Elucidation of Carbohydrate Molecular Interaction Mechanism of Recombinant and Native ArtinM

2013

[EN] The quartz crystal microbalance (QCM) technique has been applied for monitoring the biorecognition of ArtinM lectins at low horseradish peroxidase glycoprotein (HRP) concentrations, using a simple kinetic model based on Langmuir isotherm in previous work.(18) The latter approach was consistent with the data at dilute conditions but it fails to explain the small differences existing in the jArtinM and rArtinM due to ligand binding concentration limit. Here we extend this analysis to differentiate sugar-binding event of recombinant (rArtinM) and native (jArtinM) ArtinM lectins beyond dilute conditions. Equivalently, functionalized quartz crystal microbalance with dissipation monitoring (…

Models MolecularPROTEIN ADSORPTIONSURFACEKM+Horseradish peroxidaselaw.inventionsymbols.namesakelawQUARTZ-CRYSTAL MICROBALANCEBINDINGQUIMICA ANALITICAMaterials ChemistryPhysical and Theoretical ChemistrySPECIFICITYGlycoproteinsBinding SitesChromatographybiologyChemistryLectinLangmuir adsorption modelQuartz crystal microbalanceQuartz Crystal Microbalance TechniquesLECTINRecombinant ProteinsSurfaces Coatings and FilmsMannose-Binding LectinsSolvation shellHYDRATION-SHELLQuartz Crystal Microbalance TechniquesBiophysicsbiology.proteinRecombinant DNAsymbolsPlant LectinsBIOMOLECULAR ADSORPTIONARTOCARPINProtein adsorption
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Structural Mechanism of SDS-Induced Enzyme Activity of Scorpion Hemocyanin Revealed by Electron Cryomicroscopy

2009

Summary Phenoloxidases (POs) occur in all organisms and are involved in skin and hair coloring in mammals, and initiating melanization in wound healing. Mutation or overexpression of PO can cause albinism or melanoma, respectively. SDS can convert inactive PO and the oxygen carrier hemocyanin (Hc) into enzymatically active PO. Here we present single-particle cryo-EM maps at subnanometer resolution and pseudoatomic models of the 24-oligomeric Hc from scorpion Pandinus imperator in resting and SDS-activated states. Our structural analyses led to a plausible mechanism of Hc enzyme PO activation: upon SDS activation, the intrinsically flexible Hc domain I twists away from domains II and III in …

Models MolecularPROTEINSCopper proteinProtein Conformationmedicine.medical_treatmentProtein subunitArticleScorpions03 medical and health sciencesEnzyme activatorSurface-Active AgentsProtein structureStructural BiologyCatalytic DomainmedicineAnimalsBinding siteMolecular Biology030304 developmental biology0303 health sciencesBinding SitesbiologyChemistryMonophenol Monooxygenase030302 biochemistry & molecular biologyCryoelectron MicroscopyActive siteSodium Dodecyl SulfateHemocyaninEnzyme ActivationProtein SubunitsBiochemistryHemocyaninsbiology.proteinOxygen bindingStructure
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Effect of ATP Binding and Hydrolysis on Dynamics of Canine Parvovirus NS1▿ †

2010

ABSTRACT The replication protein NS1 is essential for genome replication and protein production in parvoviral infection. Many of its functions, including recognition and site-specific nicking of the viral genome, helicase activity, and transactivation of the viral capsid promoter, are dependent on ATP. An ATP-binding pocket resides in the middle of the modular NS1 protein in a superfamily 3 helicase domain. Here we have identified key ATP-binding amino acid residues in canine parvovirus (CPV) NS1 protein and mutated amino acids from the conserved A motif (K406), B motif (E444 and E445), and positively charged region (R508 and R510). All mutations prevented the formation of infectious viruse…

Models MolecularParvovirus CaninevirusesImmunologyMolecular Sequence DataPlasma protein bindingViral Nonstructural ProteinsMicrobiologyCell Linechemistry.chemical_compoundAdenosine TriphosphateDogsVirologyAnimalsAmino Acid SequenceBinding siteBinding SitesbiologyHydrolysisDNA replicationHelicaseFluorescence recovery after photobleachingFusion proteinMolecular biologyGenome Replication and Regulation of Viral Gene ExpressionProtein Structure TertiaryViral replicationchemistryBiochemistryAmino Acid SubstitutionInsect Sciencebiology.proteinCatsMutagenesis Site-DirectedSequence AlignmentDNAProtein Binding
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Synthesis of GABAA receptor agonists and evaluation of their alpha-subunit selectivity and orientation in the GABA binding site.

2008

Drugs used to treat various disorders target GABA A receptors. To develop alpha subunit selective compounds, we synthesized 5-(4-piperidyl)-3-isoxazolol (4-PIOL) derivatives. The 3-isoxazolol moiety was substituted by 1,3,5-oxadiazol-2-one, 1,3,5-oxadiazol-2-thione, and substituted 1,2,4-triazol-3-ol heterocycles with modifications to the basic piperidine substituent as well as substituents without basic nitrogen. Compounds were screened by [(3)H]muscimol binding and in patch-clamp experiments with heterologously expressed GABA A alpha ibeta 3gamma 2 receptors (i = 1-6). The effects of 5-aminomethyl-3 H-[1,3,4]oxadiazol-2-one 5d were comparable to GABA for all alpha subunit isoforms. 5-pipe…

Models MolecularPatch-Clamp TechniquesStereochemistryAlpha (ethology)gamma-Aminobutyric acidArticleGABAA-rho receptorCell Linechemistry.chemical_compoundStructure-Activity RelationshipXenopus laevisPiperidinesDrug DiscoverymedicineAnimalsHumansGABA-A Receptor AgonistsBinding siteReceptorgamma-Aminobutyric AcidG alpha subunitBinding SitesMolecular StructureChemistryGABAA receptorMuscimolBrainIsoxazolesReceptors GABA-ARatsElectrophysiologyProtein SubunitsBiochemistryMuscimolMutationOocytesMolecular MedicineFemalemedicine.drugJournal of medicinal chemistry
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Porphyrin-Based Design of Bioinspired Multitarget Quadruplex Ligands

2014

Secondary nucleic acid structures, such as DNA and RNA quadruplexes, are potential targets for cancer therapies. Ligands that interact with these targets could thus find application as anticancer agents. Synthetic G-quartets have recently found numerous applications, including use as bioinspired G-quadruplex ligands. Herein, the design, synthesis and preliminary biophysical evaluation of a new prototype multitarget G-quadruplex ligand, (PNA)PorphySQ, are reported, where peptidic nucleic acid guanine ((PNA)G) was incorporated in the porphyrin-templated synthetic G-quartet (PorphySQ). Using fluorescence resonance energy transfer (FRET)-melting experiments, PorphySQ was shown to possess enhanc…

Models MolecularPeptide Nucleic AcidsGuaninePorphyrinsStereochemistryGuanineLigands010402 general chemistryG-quadruplex01 natural sciencesBiochemistryStructure-Activity Relationship03 medical and health scienceschemistry.chemical_compoundDrug Discovery[CHIM]Chemical SciencesStructure–activity relationshipheterocyclic compoundsGeneral Pharmacology Toxicology and PharmaceuticsBinding siteComputingMilieux_MISCELLANEOUS030304 developmental biologyPharmacology0303 health sciencesBinding SitesChemistryLigandOrganic ChemistryDNA0104 chemical sciencesG-QuadruplexesFörster resonance energy transferNucleic acidNucleic Acid ConformationRNAMolecular MedicineDNAChemMedChem
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Mediation of Elicitin Activity on Tobacco Is Assumed by Elicitin-Sterol Complexes

2001

Elicitins secreted by phytopathogenic Phytophthora spp. are proteinaceous elicitors of plant defense mechanisms and were demonstrated to load, carry, and transfer sterols between membranes. The link between elicitor and sterol-loading properties was assessed with the use of site-directed mutagenesis of the 47 and 87 cryptogein tyrosine residues, postulated to be involved in sterol binding. Mutated cryptogeins were tested for their ability to load sterols, bind to plasma membrane putative receptors, and trigger biological responses. For each mutated elicitin, the chemical characterization of the corresponding complexes with stigmasterol (1:1 stoichiometry) demonstrated their full functionali…

Models MolecularPhytophthora0106 biological sciencesTime FactorsProtein Conformation[SDV]Life Sciences [q-bio]Receptors Cell SurfaceBiologyModels Biological01 natural sciencesArticleHost-Parasite InteractionsFungal Proteins03 medical and health sciencesTobaccoProtein IsoformsBinding siteReceptorMolecular BiologyComputingMilieux_MISCELLANEOUSCells CulturedPlant DiseasesPlant Proteins030304 developmental biology0303 health sciencesBinding SitesAlgal ProteinsCell MembraneProteinsElicitinCell BiologyHydrogen-Ion ConcentrationLigand (biochemistry)Receptor–ligand kineticsSterolElicitor[SDV] Life Sciences [q-bio]SterolsBiochemistryTyrosineCalciumSterol bindingProtein Binding010606 plant biology & botanyMolecular Biology of the Cell
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2NH and 3OH are crucial structural requirements in sphingomyelin for sticholysin II binding and pore formation in bilayer membranes.

2013

AbstractSticholysin II (StnII) is a pore-forming toxin from the sea anemone Stichodactyla heliantus which belongs to the large actinoporin family. The toxin binds to sphingomyelin (SM) containing membranes, and shows high binding specificity for this lipid. In this study, we have examined the role of the hydrogen bonding groups of the SM long-chain base (i.e., the 2NH and the 3OH) for StnII recognition. We prepared methylated SM-analogs which had reduced hydrogen bonding capability from 2NH and 3OH. Both surface plasmon resonance experiments, and isothermal titration calorimetry measurements indicated that StnII failed to bind to bilayers containing methylated SM-analogs, whereas clear bind…

Models MolecularPore Forming Cytotoxic ProteinsMembrane permeabilizationLipid BilayersBiophysicsCalorimetryta3111Biochemistrychemistry.chemical_compoundCnidarian VenomsAnimalsComputer SimulationLipid bilayerta116Binding selectivityUnilamellar LiposomesPhosphocholineBinding SitesMolecular StructureChemistryHydrogen bondVesicleta1182Isothermal titration calorimetryHydrogen BondingCell BiologySurface Plasmon ResonanceProtein Structure TertiarySphingomyelinsKineticsMembraneSea AnemonesBiochemistryMolecular dockingIsothermal titration calorimetryBiophysicsPhosphatidylcholinesSphingomyelinProtein BindingBiochimica et biophysica acta
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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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