Search results for "binding site"

showing 10 items of 856 documents

Prohibitin, an essential protein for Colorado potato beetle larval viability, is relevant to Bacillus thuringiensis Cry3Aa toxicity

2013

Bacillus thuringienesis (Bt) Cry toxins constitute the most extensively used environmentally safe biopesticide and their mode of action relies on the interaction of the toxins with membrane proteins in the midgut of susceptible insects that mediate toxicity and insect specificity. Therefore, identification of Bt Cry toxin interacting proteins in the midgut of target insects and understanding their role in toxicity is of great interest to exploit their insecticidal action. Using ligand blot, we demonstrated that Bt Cry3Aa toxin bound to a 30kDa protein in Colorado potato beetle (CPB) larval midgut membrane, identified by sequence homology as prohibitin-1 protein. Prohibitins comprise a highl…

ProteasesHealth Toxicology and MutagenesisBiologymedicine.disease_causeHemolysin ProteinsBacterial ProteinsRNA interferenceBacillus thuringiensisProhibitinsmedicineAnimalsProhibitinBinding siteMode of actionSolanum tuberosumBacillus thuringiensis ToxinsToxinfungiGeneral Medicinebiology.organism_classificationMolecular biologyColeopteraEndotoxinsRepressor ProteinsMembrane proteinBiochemistryLarvaAgronomy and Crop SciencePesticide Biochemistry and Physiology
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Development of Novel Selective Peptidomimetics Containing a Boronic Acid Moiety, Targeting the 20S Proteasome as Anticancer Agents

2014

This paper describes the design, synthesis, and biological evaluation of peptidomimetic boronates as inhibitors of the 20S proteasome, a validated target in the treatment of multiple myeloma. The synthesized compounds showed a good inhibitory profile against the ChT-L activity of 20S proteasome. Compounds bearing a β-alanine residue at the P2 position were the most active, that is, 3-ethylphenylamino and 4-methoxyphenylamino (R)-1-{3-[4-(substituted)-2-oxopyridin-1(2H)-yl]propanamido}-3-methylbutylboronic acids (3 c and 3 d, respectively), and these derivatives showed inhibition constants (Ki ) of 17 and 20 nM, respectively. In addition, they co-inhibited post glutamyl peptide hydrolase act…

Proteasome Endopeptidase ComplexPeptidomimeticStereochemistryCell Survivalanticancer agents; boronates; bortemib; Docking studies; Peptidomimetics; inhibitor; proteasomesAntineoplastic AgentsSaccharomyces cerevisiaedocking studieBiochemistrySubstrate Specificitychemistry.chemical_compoundCell Line TumorDrug DiscoverymedicineMoietyHumansGeneral Pharmacology Toxicology and PharmaceuticsPharmacologychemistry.chemical_classificationBinding SitesproteasomesBortezomibOrganic ChemistrybortezomibboronateBoronic AcidspeptidomimeticProtein Structure Tertiaryanticancer agentMolecular Docking SimulationinhibitorEnzymechemistryProteasomeBiochemistryDocking (molecular)Molecular MedicinePeptidomimeticsGrowth inhibitionDrug Screening Assays AntitumorProteasome InhibitorsBoronic acidmedicine.drug
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Immunoproteasome and Non-Covalent Inhibition: Exploration by Advanced Molecular Dynamics and Docking Methods

2021

The selective inhibition of immunoproteasome is a valuable strategy to treat autoimmune, inflammatory diseases, and hematologic malignancies. Recently, a new series of amide derivatives as non-covalent inhibitors of the β1i subunit with Ki values in the low/submicromolar ranges have been identified. Here, we investigated the binding mechanism of the most potent and selective inhibitor, N-benzyl-2-(2-oxopyridin-1(2H)-yl)propanamide (1), to elucidate the steps from the ligand entrance into the binding pocket to the ligand-induced conformational changes. We carried out a total of 400 ns of MD-binding analyses, followed by 200 ns of plain MD. The trajectories clustering allowed identifying thre…

Proteasome Endopeptidase ComplexStereochemistryPharmaceutical ScienceOrganic chemistryinduced-fit dockingMolecular Dynamics Simulation01 natural sciencesArticlemetadynamicsAnalytical Chemistry03 medical and health scienceschemistry.chemical_compoundimmunoproteasomeQD241-441AmideDrug DiscoveryOrganosilicon CompoundsPhysical and Theoretical Chemistrynon-covalent inhibitor030304 developmental biology0303 health sciencesBinding Sites010405 organic chemistrymolecular dynamicnon-covalent inhibitorsMetadynamicsRational designDipeptidesLigand (biochemistry)PropanamideSettore CHIM/08 - Chimica Farmaceuticamolecular dynamics0104 chemical sciencesMolecular Docking SimulationchemistryChemistry (miscellaneous)Docking (molecular)MD bindingMolecular MedicinemetadynamicLead compoundOligopeptidesProteasome InhibitorsAcetamideProtein BindingMolecules
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Kinetic analysis and molecular modeling of the inhibition mechanism of roneparstat (SST0001) on human heparanase

2016

Heparanase is a β-d-glucuronidase which cleaves heparan sulfate chains in the extracellular matrix and on cellular membranes. A dysregulated heparanase activity is intimately associated with cell invasion, tumor metastasis and angiogenesis, making heparanase an attractive target for the development of anticancer therapies. SST0001 (roneparstat; Sigma-Tau Research Switzerland S.A.) is a non-anticoagulant 100% N-acetylated and glycol-split heparin acting as a potent heparanase inhibitor, currently in phase I in advanced multiple myeloma. Herein, the kinetics of heparanase inhibition by roneparstat is reported. The analysis of dose-inhibition curves confirmed the high potency of roneparstat (I…

Protein Conformation alpha-Helical0301 basic medicineSST0001Molecular modelhomology modelingAmino Acid MotifsPlasma protein bindingMolecular Dynamics SimulationBiochemistryMolecular Docking SimulationheparanaseSubstrate Specificity03 medical and health scienceschemistry.chemical_compound0302 clinical medicinePolysaccharidesHumansProtein Interaction Domains and MotifsHeparanaseHomology modelingEnzyme InhibitorsGlucuronidaseBinding Siteskinetic inhibition analysisHeparinComputational BiologyHeparan sulfateRecombinant ProteinsAcidobacteriaMolecular Docking SimulationEnzyme bindingKinetics030104 developmental biologyCarbohydrate SequenceFondaparinuxchemistryBiochemistryStructural Homology ProteinDocking (molecular)030220 oncology & carcinogenesisBiophysicsroneparstatThermodynamicsProtein Conformation beta-StrandORIGINAL ARTICLESProtein BindingGlycobiology
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A potential solution to avoid overdose of mixed drugs in the event of Covid-19: Nanomedicine at the heart of the Covid-19 pandemic.

2021

Since 2020, the world is facing the first global pandemic of 21st century. Among all the solutions proposed to treat this new strain of coronavirus, named SARS-CoV-2, the vaccine seems a promising way but the delays are too long to be implemented quickly. In the emergency, a dual therapy has shown its effectiveness but has also provoked a set of debates around the dangerousness of a particular molecule, hydroxychloroquine. In particular, the doses to be delivered, according to the studies, were well beyond the acceptable doses to support the treatment without side effects. We propose here to use all the advantages of nanovectorization to address this question of concentration. Using quantum…

Protein Conformation alpha-HelicalComputer science02 engineering and technologyAzithromycinDrug Delivery SystemsPandemicMaterials ChemistryDrug Dosage CalculationsSpectroscopymedia_common0303 health sciencesEvent (computing)021001 nanoscience & nanotechnologyComputer Graphics and Computer-Aided DesignMolecular Docking SimulationNanomedicineRisk analysis (engineering)Spike Glycoprotein CoronavirusDensity functional theory calculationsNanomedicineThermodynamicsNitrogen OxidesAngiotensin-Converting Enzyme 20210 nano-technologyHydroxychloroquineProtein BindingDrugBoron CompoundsCoronavirus disease 2019 (COVID-19)media_common.quotation_subjectSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)Molecular Dynamics SimulationAntiviral AgentsArticle03 medical and health sciencesHumansProtein Interaction Domains and MotifsDual therapyPhysical and Theoretical Chemistry030304 developmental biologyDrug transportBinding SitesSARS-CoV-2Molecular dynamics simulationsCOVID-19NanostructuresCOVID-19 Drug TreatmentKineticsQuantum TheoryProtein Conformation beta-StrandNanovectorizationJournal of molecular graphicsmodelling
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High affinity agonistic metal ion binding sites within the melanocortin 4 receptor illustrate conformational change of transmembrane region 3.

2003

We created a molecular model of the human melanocortin 4 receptor (MC4R) and introduced a series of His residues into the receptor protein to form metal ion binding sites. We were able to insert micromolar affinity binding sites for zinc between transmembrane region (TM) 2 and TM3 where the metal ion alone was able to activate this peptide binding G-protein-coupled receptor. The exact conformation of the metal ion interactions allowed us to predict the orientation of the helices, and remodeling of the receptor protein indicated that Glu100 and Ile104 in TM2 and Asp122 and Ile125 in TM3 are directed toward a putative area of activation of the receptor. The molecular model suggests that a rot…

Protein ConformationAmino Acid MotifsPeptide bindingPlasma protein bindingTransfectionBiochemistryCell LineReceptors G-Protein-CoupledProtein structureCyclic AMPHumansPoint MutationBinding siteReceptorMolecular BiologyBinding SitesChemistryMembrane ProteinsCell BiologyMelanocortin 4 receptorCytosolic partZincBiochemistryBiophysicsReceptor Melanocortin Type 4MelanocortinProtein BindingThe Journal of biological chemistry
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Molecular dynamics studies on Mdm2 complexes: An analysis of the inhibitor influence

2012

p53 is a powerful anti-tumoral molecule frequently inactivated by mutations or deletions in cancer. However, half of all human tumors expresses wild-type p53, and its activation, by antagonizing its negative regulator Mdm2, might offer a new strategy for therapeutic protocol. In this work, we present a molecular dynamics study on Mdm2 structure bound to two different known inhibitors with the aim to investigate the structural transitions between apo-Mdm2 and Mdm2-inhibitor complexes. We tried to gain information about conformational changes binding a benzodiazepine derivative inhibitor with respect the known nutlin and the apo form. The conformational changes alter the size of the cleft and…

Protein ConformationBiophysicsMolecular Dynamics SimulationMdm2 p53 nutlin benzodiazepine Molecular DynamicsBiochemistryNegative regulatorBenzodiazepineschemistry.chemical_compoundMolecular dynamicsHumansMoleculeEnzyme InhibitorsMolecular BiologyBinding SitesbiologyChemistryProto-Oncogene Proteins c-mdm2Cell BiologyNutlinSettore CHIM/08 - Chimica FarmaceuticaBiochemistryDrug DesignBiophysicsbiology.proteinMdm2LinkerBiochemical and Biophysical Research Communications
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Bishistidyl heme hexacoordination, a key structural property in Drosophila melanogaster hemoglobin

2005

Hemoglobins at high concentration have been isolated long ago from some insect larvae living in hypoxic environments. Conversely, a monomeric hemoglobin has been discovered recently in the fruit fly Drosophila melanogaster as intracellular protein expressed both in larvae and in the adult fly. Such a finding indicates that the oxygen supply in insects may be more complex than previously thought, relying not only on O2 diffusion through the tubular tracheal system, but also on carrier-mediated transport and storage. We present here the crystal structure of recombinant D. melanogaster hemoglobin at 1.20 A resolution. Spectroscopic data show that the protein displays a hexacoordinated heme, wh…

Protein ConformationHemeMatrix (biology)BiologyCrystallography X-RayLigandsBiochemistrylaw.inventionchemistry.chemical_compoundHemoglobinslawMelanogasterAnimalsDrosophila ProteinsHistidineMolecular BiologyHemeCyclohexylaminesBinding SitesSpectrum AnalysisfungiCell BiologyHEXAbiology.organism_classificationOxygenMyoglobinchemistryBiochemistryAlkanesulfonic AcidsBiophysicsRecombinant DNAHemoglobinDrosophila melanogaster
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PLA2-mediated catalytic activation of its inhibitor 25-acetyl-petrosaspongiolide M: serendipitous identification of a new PLA2 suicide inhibitor.

2004

Abstract25-Acetyl-petrosaspongiolide M (PMAc) (1), a mild non-covalent PLA2 inhibitor, unexpectedly recovers, after incubation with bvPLA2, the ability to covalently modify the enzyme target. This study demonstrates the catalytic effect of bvPLA2 in converting 1 in its deacetylated congener petrosaspongiolide M (PM) (2), a strong covalent PLA2 inhibitor whose molecular mechanism of inhibition has already been clarified. Moreover, our findings outline the potential role of PMAc as anti-inflammatory pro-drug, by virtue of its ability of delivering the active PM agent at the site of inflammation, functioning as a suicide inhibitor.

Protein ConformationMarine natural productLigandsBiochemistryMass SpectrometryProtein Structure SecondaryCIRCULAR-DICHROISMchemistry.chemical_compoundProtein structureStructural BiologyBINDINGEnzyme InhibitorsChromatography High Pressure Liquidchemistry.chemical_classificationbiologyMolecular StructureChemistryCircular DichroismHydrolysisTemperatureAcetylationHydrogen-Ion ConcentrationBEE VENOM PHOSPHOLIPASE-A2PoriferaPETROSASPONGIOLIDES M-RBiochemistryCovalent bondINACTIVATIONMANOALIDESpectrometry Mass Electrospray IonizationCYTOSOLIC PHOSPHOLIPASE A(2); BEE VENOM PHOSPHOLIPASE-A2; FLUORESCENCE DISPLACEMENT ASSAY; PETROSASPONGIOLIDES M-R; CIRCULAR-DICHROISM; NATURAL-PRODUCTS; INACTIVATION; MANOALIDE; POTENT; BINDINGStereochemistryBiophysicsGroup II Phospholipases A2CatalysisPhospholipases AAnti-inflammatory compoundManoalidePhospholipase A2NATURAL-PRODUCTSGeneticsTrifluoroacetic acidAnimalsBinding siteOleanolic AcidMolecular BiologyBinding SitesPOTENTCYTOSOLIC PHOSPHOLIPASE A(2)Cell BiologyMolecular WeightKineticsPhospholipases A2EnzymeAcetylationbiology.proteinFLUORESCENCE DISPLACEMENT ASSAYPhospholipase A2 inhibitionFEBS letters
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Activation of the p75 neurotrophin receptor through conformational rearrangement of disulphide-linked receptor dimers.

2009

Ligand-mediated dimerization has emerged as a universal mechanism of growth factor receptor activation. Recent structural studies have shown that neurotrophins interact with dimers of the p75 neurotrophin receptor (p75NTR), but the actual mechanism of receptor activation has remained elusive. Here we show that p75NTR forms disulphide-linked dimers independently of neurotrophin binding through the highly conserved Cys257 in its transmembrane domain. Mutation of Cys257 abolished neurotrophin-dependent receptor activity but did not affect downstream signaling by the p75NTR/NgR/Lingo-1 complex in response to MAG, indicating the existence of distinct, ligand-specific activation mechanisms for p7…

Protein ConformationMutantNeuronesReceptor Nerve Growth FactorMiceProtein structureChlorocebus aethiopsNerve Growth FactorLow-affinity nerve growth factor receptorRNA Small InterferingReceptorskin and connective tissue diseasesReceptors neuralsCells CulturedNeuronsCell DeathGeneral NeuroscienceNF-kappa BCell biologyTransmembrane domainSIGNALINGOligopeptidesNeurotrophinProtein BindingSignal Transductionmusculoskeletal diseasesPROTEINSNeuroscience(all)Green Fluorescent ProteinsNerve Tissue ProteinsReceptors Nerve Growth FactorSuperior Cervical GanglionBiologyTransfectionMOLNEUROArticleGrowth factor receptorAnimalsHumansProtein Interaction Domains and MotifsReceptors Growth FactorCysteineBinding SitesMembrane Proteinsbiological factorsRatsnervous systemAnimals NewbornNeurotrophin bindingMutationbiology.proteinsense organsProtein MultimerizationrhoA GTP-Binding ProteinProteïnesNeuron
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