Search results for "binding sites"

showing 10 items of 636 documents

Structure of SNX9 SH3 in complex with a viral ligand reveals the molecular basis of its unique specificity for alanine-containing class I SH3 motifs

2021

Class I SH3 domain-binding motifs generally comply with the consensus sequence [R/K]x0PxxP, the hydrophobic residue 0 being proline or leucine. We have studied the unusual 0 = Ala-specificity of SNX9 SH3 by determining its complex structure with a peptide present in eastern equine encephalitis virus (EEEV) nsP3. The structure revealed the length and composition of the n-Src loop as important factors determining specificity. We also compared the affinities of EEEV nsP3 peptide, its mutants, and cellular ligands to SNX9 SH3. These data suggest that nsP3 has evolved to minimize reduction of conformational entropy upon binding, hence acquiring stronger affinity, enabling takeover of SNX9. The R…

DYNAMICSPROLINE-RICH PEPTIDESviruksetPROTEINSvirusesHTLV-1 GagLigandsEVOLUTIONARY CONSERVATIONalfaviruksetsrc Homology DomainsHIGH-AFFINITYretroviruksetDOMAINStructural BiologyBINDINGAnimalsHorsesMolecular Biologysoluviestintä11832 Microbiology and virologyAlanineBinding SitesPXXP MOTIFSisothermal titration calorimetrySH3solution NMR spectroscopyEEEV nsP3HIV-11182 Biochemistry cell and molecular biologyproteiinitCHEMICAL-SHIFTS3111 BiomedicinePeptidesSNX9Protein Binding
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Principal component analysis on molecular descriptors as an alternative point of view in the search of new Hsp90 inhibitors

2009

Inhibiting a protein that regulates multiple signal transduction pathways in cancer cells is an attractive goal for cancer therapy. Heat shock protein 90 (Hsp90) is one of the most promising molecular targets for such an approach. In fact, Hsp90 is a ubiquitous molecular chaperone protein that is involved in folding, activating and assembling of many key mediators of signal transduction, cellular growth, differentiation, stress-response and apoptothic pathways. With the aim to analyze which molecular descriptors have the higher importance in the binding interactions of these classes, we first performed molecular docking experiments on the 187 Hsp90 inhibitors included in the BindingDB, a pu…

Databases FactualProtein ConformationDrug Evaluation PreclinicalCancer therapyPrincipal component analysiNaphtholsBiochemistryBinding databaseMolecular descriptorsStructure-Activity RelationshipStructural BiologyMolecular descriptorHeat shock proteinComputer SimulationHSP90 Heat-Shock ProteinsPrincipal Component AnalysisBinding SitesbiologyHeat shock proteinOrganic ChemistryComputational BiologyIsoxazolesHsp90Settore CHIM/08 - Chimica FarmaceuticaComputational MathematicsBiochemistryPurinesDocking (molecular)Principal component analysisMolecular dockingbiology.proteinPyrazolesBindingDBSignal transduction
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DNA binding, nuclease activity, DNA photocleavage and cytotoxic properties of Cu(II) complexes of N-substituted sulfonamides.

2013

Abstract Ternary copper(II) complexes [Cu(NST)2(phen)] (1) and [Cu(NST)2(NH3)2]·H2O (2) [HNST = N-(4,5-dimethylthiazol-2-yl)naphthalene-1-sulfonamide] were prepared and characterized by physico-chemical techniques. Both 1 and 2 were structurally characterized by X-ray crystallography. The crystal structures show the presence of a distorted square planar CuN4 geometry in which the deprotonated sulfonamide, acting as monodentate ligand, binds to the metal ion through the thiazole N atom. Both complexes present intermolecular π–π stacking interactions between phenanthroline rings (compound 1) and between naphthalene rings (compound 2). The interaction of the complexes with CT DNA was studied b…

DenticityStereochemistryCell SurvivalUltraviolet RaysPhenanthrolineRadicalStackingAscorbic AcidNaphthalenesBiochemistryFluorescence spectroscopyInorganic Chemistrychemistry.chemical_compoundInhibitory Concentration 50Coordination ComplexesCell Line TumorAnimalsHumansDNA CleavageThiazoleNucleaseSulfonamidesBinding SitesbiologyCytotoxinsHydroxyl RadicalDNAHydrogen PeroxidePhotochemical ProcessesKineticschemistrybiology.proteinCattleDNACopperPhenanthrolinesJournal of inorganic biochemistry
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Extracellular site of action of phenylalkylamines on L-type calcium current in rat ventricular myocytes.

1995

The effects of the phenylalkylamines verapamil, gallopamil, and devapamil on L-type calcium currents (ICa) were studied in ventricular myocytes from rat hearts using the whole-cell patch-clamp technique. In particular, the question was addressed, whether the pharmacological binding sites for these drugs were located at the inner and/or at the outer surface of the cell membrane. Therefore, tertiary verapamil, gallopamil, and devapamil and their corresponding quaternary derivatives were applied either from the outside or the inside of the cell membrane. Extracellular application of verapamil, gallopamil and devapamil (each at 3 microM) reduced ICa to 16.1 +/- 8.6%, 11 +/- 8.9%, and 9.3 +/- 6%…

DevapamilGallopamilPatch-Clamp TechniquesHeart Ventricleschemistry.chemical_elementPharmacologyCalciumRats Sprague-Dawleychemistry.chemical_compoundmedicineExtracellularAnimalsPatch clampGallopamilPharmacologyBinding SitesChemistryCalcium channelCell MembraneGeneral MedicineCalcium Channel BlockersRatsVerapamilcardiovascular systemVerapamilCalcium ChannelsIntracellularmedicine.drugNaunyn-Schmiedeberg's archives of pharmacology
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Induction of digoxin-like material production, and the digoxin binding in the unicellular organism Tetrahymena by digitoxin.

1998

Thin layer chromatographic, and laser-confocal microscopic analyses with a monoclonal antibody to digoxin also displaying high affinity to digoxigenin, were used to determine the presence and localization of cardioactive glycosides. Tetrahymena pyriformis was found to possess digitoxigenin-like material, but digoxin, digitoxin, digoxigenin, gitoxin and lanatoside C were not detected. Digitoxin treatment elicited the appearance of a digoxin-like material in the progeny generations. Digoxin was taken up by untreated Tetrahymena, especially strongly 24 h after digitoxin treatment. While the cardenolide was localized in vesicles of the cell body in untreated Tetrahymena, the engulfed digoxin ap…

DigoxinDigoxinDigitoxinBiologychemistry.chemical_compoundDigitoxinpolycyclic compoundsmedicineCardenolideDigoxigeninAnimalscardiovascular diseasesChromatography High Pressure Liquidchemistry.chemical_classificationBinding SitesMicroscopy ConfocalTetrahymena pyriformisdigestive oral and skin physiologyCell MembraneLanatoside CTetrahymenaDigitalis GlycosidesBiological TransportCell BiologyGeneral Medicinebiology.organism_classificationImmunohistochemistrycarbohydrates (lipids)EnzymechemistryBiochemistryTetrahymena pyriformiscirculatory and respiratory physiologymedicine.drugCell biology international
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DNA-binding studies of AV-153, an antimutagenic and DNA repair-stimulating derivative of 1,4-dihydropiridine.

2014

Abstract The ability to intercalate between DNA strands determines the cytotoxic activity of numerous anticancer drugs. Strikingly, intercalating activity was also reported for some compounds considered to be antimutagenic. The aim of this study was to determine the mode of interaction of DNA with the antimutagenic and DNA repair-stimulating dihydropyridine (DHP) AV-153. DNA and AV-153 interactions were studied by means of UV/VIS spectroscopy, fluorimetry and infrared spectroscopy. Compound AV-153 is a 1,4 dihydropyridine with ethoxycarbonyl groups in positions 3 and 5. Computer modeling of AV-153 and DNA interactions suggested an ability of the compound to dock between DNA strands at a sin…

DihydropyridinesBinding SitesDNA RepairMolecular StructureGuanineDNA repairStereochemistryAntimutagenic AgentsGeneral MedicineDNAToxicologyNiacinThymineRatschemistry.chemical_compoundPlasmidDNA IntercalationchemistryLiverSpectroscopy Fourier Transform InfraredAnimalsA-DNACytosineDNAChemico-biological interactions
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Dual-affinity avidin molecules

2005

A recently reported dual-chain avidin was modified further to contain two distinct, independent types of ligand-binding sites within a single polypeptide chain. Chicken avidin is normally a tetrameric glycoprotein that binds water-soluble d-biotin with extreme affinity (Kd ≈ 10−15M). Avidin is utilized in various applications and techniques in the life sciences and in the nanosciences. In a recent study, we described a novel avidin monomer-fusion chimera that joins two circularly permuted monomers into a single polypeptide chain. Two of these dual-chain avidins were observed to associate spontaneously to form a dimer equivalent to the wt tetramer. In the present study, we successfully used …

DimerBiochemistryChromatography AffinityProtein Structure Secondarychemistry.chemical_compoundBiotinAffinity chromatographyTetramerStructural BiologyAnimalsBinding siteMolecular BiologyFluorescent Dyeschemistry.chemical_classificationBinding SitesbiologyChemistryTemperatureAvidinBiochemistryBiotinylationbiology.proteinThermodynamicsGlycoproteinChickensProtein BindingAvidinProteins: Structure, Function, and Bioinformatics
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Calcium-binding sites in the inner ear after pure-tone stimulation

1991

Five guinea pigs were exposed to an interrupted 90 dB SPL pure tone of 3.2 kHz for a total application time of 5 min. Following sound application all animals were decapitated and the cochleae were removed. After that, calcium-binding sites were located by the potassium pyroantimonate precipitation method. Another three animals served as control animals and did not receive the sound treatment. Findings confirmed previous studies showing the spatial arrangements of precipitate rich regions in the inner ear's two acellular structures (the basilar membrane and tectorial membrane) and the two cellular structures (the inner hair cells and Huschke's teeth). By using semiquantitative evaluation we …

DiminutionBinding SitesTectorial membraneGuinea Pigschemistry.chemical_elementStimulationGeneral MedicineAnatomyCalciumBiologyGuinea pigBasilar membraneSoundmedicine.anatomical_structureAcoustic StimulationOtorhinolaryngologychemistryEar Innerotorhinolaryngologic diseasesmedicineAnimalsCalciumInner earsense organsBinding siteEuropean Archives of Oto-Rhino-Laryngology
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A high-quality homology model for the human dopamine transporter validated for drug design purposes.

2018

The human dopamine transporter (hDAT) plays many vital functions within the central nervous system and is thus targeted by many pharmaceutical agents. Dopamine-related therapies are in current development for individuals with dopamine-related disorders including depression, Parkinson's disease, and psychostimulant addictions such as cocaine abuse. Yet, most efforts to develop new dopamine therapies are within costly structure-activity relationship studies. Through structure-based drug design techniques, the binding site of hDAT can be utilized to develop novel selective and potent dopamine therapies at reduced costs. However, no structural models of hDAT specifically validated for rational …

DrugComputer sciencemedia_common.quotation_subjectDrug designComputational biologyNortriptyline01 natural sciencesBiochemistryInhibitory Concentration 50DopamineDrug DiscoverymedicineAnimalsDrosophila ProteinsHumansHomology modelingmedia_commonDopamine transporterPharmacologyDopamine Plasma Membrane Transport ProteinsBinding Sitesbiology010405 organic chemistryAddictionOrganic Chemistry0104 chemical sciencesProtein Structure TertiaryMolecular Docking Simulation010404 medicinal & biomolecular chemistryDrug Designbiology.proteinMolecular MedicineDrosophilaCocaine abusemedicine.drugChemical biologydrug design
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Microscopic interactions between ivermectin and key human and viral proteins involved in SARS-CoV-2 infection

2021

The identification of chemical compounds able to bind specific sites of the human/viral proteins involved in the SARS-CoV-2 infection cycle is a prerequisite to design effective antiviral drugs. Here we conduct a molecular dynamics study with the aim to assess the interactions of ivermectin, an antiparasitic drug with broad-spectrum antiviral activity, with the human Angiotensin-Converting Enzyme 2 (ACE2), the viral 3CLpro and PLpro proteases, and the viral SARS Unique Domain (SUD). The drug/target interactions have been characterized in silico by describing the nature of the non-covalent interactions found and by measuring the extent of their time duration along the MD simulation. Results …

DrugProteasesIn silicomedia_common.quotation_subjectProtein domainCoronavirus Papain-Like ProteasesGeneral Physics and AstronomyPlasma protein bindingBiologyAntiviral AgentsivermectinProtein DomainsMolecular dynamics simulationHumansPhysical and Theoretical ChemistryBinding siteCoronavirus 3C Proteasesmedia_commonchemistry.chemical_classificationSARS Unique DomainBinding SitesSARS-CoV-2SARS-CoV-2 infectionRNAHydrogen BondingVirologyG-QuadruplexesMolecular Docking SimulationEnzymechemistrySettore CHIM/03 - Chimica Generale E InorganicaRNAAngiotensin-Converting Enzyme 2Hydrophobic and Hydrophilic InteractionsProtein BindingPhysical Chemistry Chemical Physics
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