Search results for "protein conformation"

showing 10 items of 515 documents

Conf-VLKA: A structure-based revisitation of the Virtual Lock-and-key Approach

2016

In a previous work, we developed the in house Virtual Lock-and-Key Approach (VLKA) in order to evaluate target assignment starting from molecular descriptors calculated on known inhibitors used as an information source. This protocol was able to predict the correct biological target for the whole dataset with a good degree of reliability (80%), and proved experimentally, which was useful for the target fishing of unknown compounds. In this paper, we tried to remodel the previous in house developed VLKA in a more sophisticated one in order to evaluate the influence of 3D conformation of ligands on the accuracy of the prediction. We applied the same previous algorithm of scoring and ranking b…

0301 basic medicineMaterials Chemistry2506 Metals and AlloysInhibitorStructure-basedComputer scienceProtein ConformationProtein Data Bank (RCSB PDB)Molecular ConformationTarget fishingMolecular Dynamics Simulationcomputer.software_genreLigands01 natural sciencesDockingVlka03 medical and health sciencesMolecular descriptorMaterials ChemistryHumansPhysical and Theoretical ChemistryCluster analysisDatabases ProteinSimulationSpectroscopyBinding SitesProteinscomputer.file_formatDescriptorProtein Data BankComputer Graphics and Computer-Aided Design0104 chemical sciencesMolecular Docking Simulation010404 medicinal & biomolecular chemistry030104 developmental biologyProtein–ligand dockingBiological targetDocking (molecular)Biological targetStructure basedLigand-basedData miningcomputerAlgorithmsSoftwareProtein Binding
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The malate sensing two-component system MaeKR is a non-canonical class of sensory complex for C4-dicarboxylates

2017

16 páginas, 7 figuras, 2 tablas

0301 basic medicineModels MolecularAdenosine Triphosphate / metabolismProtein ConformationScienceMalatesBacterial proteins/chemistry/metabolism/geneticsPlasma protein bindingBiologyModels BiologicalArticleConserved sequence03 medical and health sciencesAdenosine TriphosphateBacterial ProteinsAdenosine Triphosphate / chemistryDicarboxylic AcidsProtein Interaction Domains and MotifsAmino Acid SequenceKinase activityPhosphorylationLactobacilus cassei/classification/physiologyMalates/metabolismPromoter Regions GeneticConserved SequencePhylogenyMultidisciplinaryQAutophosphorylationfungiRTwo-component regulatory systemResponse regulatorLacticaseibacillus casei030104 developmental biologyBiochemistryMedicineModelsbiologica/moleculPhosphorylationCconserved secuenceProtein MultimerizationBinding domainProtein BindingScientific Reports
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Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases

2020

13 páginas, 6 figuras, 3 tablas

0301 basic medicineModels MolecularBioquímicaHistidine KinaseProtein ConformationScience030106 microbiologyPhosphataseGeneral Physics and AstronomyMicrobiologiaCrystallography X-RayModels BiologicalBiochemistryMicrobiologyGeneral Biochemistry Genetics and Molecular BiologyCatalysisArticleEnzyme catalysis03 medical and health sciencesResidue (chemistry)Protein structureBacterial ProteinsMultienzyme ComplexesHistidineThermotoga maritimaPhosphorylationlcsh:ScienceAuthor CorrectionHistidineX-ray crystallographyMultidisciplinaryEffectorChemistryEscherichia coli ProteinsQGeneral ChemistryHydrogen-Ion ConcentrationResponse regulator030104 developmental biologyBiochemistryMutationTrans-ActivatorsPhosphorylationlcsh:QBacterial Outer Membrane Proteins
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High-Pressure-Driven Reversible Dissociation of α-Synuclein Fibrils Reveals Structural Hierarchy

2017

The analysis of the α-synuclein (aS) aggregation process, which is involved in Parkinson's disease etiopathogenesis, and of the structural feature of the resulting amyloid fibrils may shed light on the relationship between the structure of aS aggregates and their toxicity. This may be considered a paradigm of the ground work needed to tackle the molecular basis of all the protein-aggregation-related diseases. With this aim, we used chemical and physical dissociation methods to explore the structural organization of wild-type aS fibrils. High pressure (in the kbar range) and alkaline pH were used to disassemble fibrils to collect information on the hierarchic pathway by which distinct β-sh…

0301 basic medicineModels MolecularCircular dichroismAmyloidProtein FoldingProtein domainBeta sheetBiophysicsFibrilMicroscopy Atomic ForceSpectrum Analysis RamanDissociation (chemistry)03 medical and health sciences0302 clinical medicineProtein structureMicroscopy Electron TransmissionProtein DomainsSpectroscopy Fourier Transform InfraredEscherichia coliPressureChemistryCircular DichroismEnergy landscapeProteinsalpha synuclein amyloid recombinant proteinHydrogen-Ion ConcentrationRecombinant ProteinsCrystallography030104 developmental biologyMutationalpha-SynucleinProtein foldingProtein Conformation beta-StrandProtein Multimerization030217 neurology & neurosurgery
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On the (un)coupling of the chromophore, tongue interactions, and overall conformation in a bacterial phytochrome

2018

Phytochromes are photoreceptors in plants, fungi, and various microorganisms and cycle between metastable red light-absorbing (Pr) and far-red light-absorbing (Pfr) states. Their light responses are thought to follow a conserved structural mechanism that is triggered by isomerization of the chromophore. Downstream structural changes involve refolding of the so-called tongue extension of the phytochrome-specific GAF-related (PHY) domain of the photoreceptor. The tongue is connected to the chromophore by conserved DIP and PRXSF motifs and a conserved tyrosine, but the role of these residues in signal transduction is not clear. Here, we examine the tongue interactions and their interplay with …

0301 basic medicineModels MolecularCrystallography X-RayBiochemistrybakteeritProtein structurephotoconversionchromophore-binding domainTransferasestructural biologyCRYSTAL-STRUCTURETyrosineDEINOCOCCUS-RADIODURANSbiologyPhytochromeChemistryREARRANGEMENTSProtein Structure and FoldingDeinococcusmutagenesisBinding domainSignal TransductionMODULEPLANT PHYTOCHROMEPhenylalaninefotobiologia03 medical and health sciencesBacterial Proteinsprotein conformationcell signalingprotein structureBACTERIOPHYTOCHROMEMolecular BiologyX-ray crystallographysoluviestintäphytochromeAGP1BINDING DOMAINBinding Sitesta114030102 biochemistry & molecular biologyta1182Deinococcus radioduransCell BiologyChromophorebiology.organism_classificationphotoreceptor030104 developmental biologyStructural biologyFTIRBiophysicsTyrosineproteiinit3111 Biomedicineröntgenkristallografia
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Probing Differential Binding Mechanisms of Phenylalanine-Glycine-Rich Nucleoporins by Single-Molecule FRET

2018

Abstract Phenylalanine-glycine-rich nucleoporins (FG-Nups) are intrinsically disordered proteins, constituting the selective barrier of the nuclear pore complex. They are highly dynamic under physiological conditions and studying their interaction with nuclear transport receptors (NTRs) is key to understanding the molecular mechanism of nucleocytoplasmic transport. Distinct conformational features of FG-Nups interacting with diverse NTRs can be detected by multiparameter single-molecule fluorescence energy transfer (smFRET), which is a powerful technique for studying the dynamics and interactions of biomolecules in solution. Here we provide a detailed protocol utilizing smFRET to reveal dif…

0301 basic medicineModels MolecularGlycosylationProtein ConformationPhenylalanineGlycineIntrinsically disordered proteinsArticle03 medical and health scienceschemistry.chemical_compoundFluorescence Resonance Energy TransferAnimalsHumansNuclear porechemistry.chemical_classificationBiomoleculeSingle-molecule FRETEquipment DesignIntrinsically Disordered ProteinsNuclear Pore Complex Proteins030104 developmental biologychemistryNucleocytoplasmic TransportBiophysicsNucleoporinNuclear transportProtein BindingIntrinsically Disordered Proteins
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Two differential binding mechanisms of FG-nucleoporins and nuclear transport receptors

2018

Summary Phenylalanine-glycine-rich nucleoporins (FG-Nups) are intrinsically disordered proteins, constituting the selective barrier of the nuclear pore complex (NPC). Previous studies showed that nuclear transport receptors (NTRs) were found to interact with FG-Nups by forming an “archetypal-fuzzy” complex through the rapid formation and breakage of interactions with many individual FG motifs. Here, we use single-molecule studies combined with atomistic simulations to show that, in sharp contrast, FG-Nup214 undergoes a coupled reconfiguration-binding mechanism when interacting with the export receptor CRM1. Association and dissociation rate constants are more than an order of magnitude lowe…

0301 basic medicineModels MolecularGlycosylationglycosylationProtein ConformationPhenylalanineGlycineSequence (biology)Intrinsically disordered proteinsnuclear transport receptorssingle-molecule FRETGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health scienceschemistry.chemical_compound0302 clinical medicineEscherichia coliFluorescence Resonance Energy TransferHumansNuclear poreReceptorlcsh:QH301-705.5Single-molecule FRETmolecular dynamics simulationsbinding mechanismintrinsically disordered proteinFG-Nup3. Good healthNuclear Pore Complex Proteins030104 developmental biologychemistrylcsh:Biology (General)BiophysicsNuclear PoreNucleoporinNuclear transport030217 neurology & neurosurgeryProtein BindingCell Reports
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rbFOX1/MBNL1 competition for CCUG RNA repeats binding contributes to myotonic dystrophy type 1/type 2 differences

2018

Myotonic dystrophy type 1 and type 2 (DM1, DM2) are caused by expansions of CTG and CCTG repeats, respectively. RNAs containing expanded CUG or CCUG repeats interfere with the metabolism of other RNAs through titration of the Muscleblind-like (MBNL) RNA binding proteins. DM2 follows a more favorable clinical course than DM1, suggesting that specific modifiers may modulate DM severity. Here, we report that the rbFOX1 RNA binding protein binds to expanded CCUG RNA repeats, but not to expanded CUG RNA repeats. Interestingly, rbFOX1 competes with MBNL1 for binding to CCUG expanded repeats and overexpression of rbFOX1 partly releases MBNL1 from sequestration within CCUG RNA foci in DM2 muscle ce…

0301 basic medicineModels MolecularProtein Conformation alpha-Helical[SDV]Life Sciences [q-bio]General Physics and AstronomyGene ExpressionRNA-binding proteinCrystallography X-Raychemistry.chemical_compoundMOLECULAR-BASISGene expressionMBNL1Myotonic DystrophyComputingMilieux_MISCELLANEOUSMultidisciplinaryCHLORIDE CHANNELQRNA-Binding ProteinsRecombinant Proteins3. Good healthCell biologyCONGENITAL HEART-DISEASEDrosophila melanogasterThermodynamicsSKELETAL-MUSCLERNA Splicing FactorsCUG REPEATSProtein BindingRNA Splicing Factorsmusculoskeletal diseasesSTEADY-STATEcongenital hereditary and neonatal diseases and abnormalitiesScienceRBFOX1BiologyMyotonic dystrophyBinding CompetitiveGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciencesmedicineEscherichia coliAnimalsHumansProtein Interaction Domains and MotifsBinding siteNucleotide MotifsMuscle SkeletalSPLICING REGULATOR RBFOX2MUSCLEBLIND PROTEINSBinding SitesPRE-MESSENGER-RNARNAGeneral Chemistrymedicine.diseaseDisease Models AnimalKinetics030104 developmental biologychemistryTRIPLET REPEATRNAProtein Conformation beta-Strand3111 Biomedicine
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Bioactive triterpenes of protium heptaphyllum gum resin extract display cholesterol-lowering potential

2021

Hypercholesterolemia is one of the major causes of cardiovascular disease, the risk of which is further increased if other forms of dyslipidemia occur. Current therapeutic strategies include changes in lifestyle coupled with drug administration. Statins represent the most common therapeutic approach, but they may be insufficient due to the onset of resistance mechanisms and side effects. Consequently, patients with mild hypercholesterolemia prefer the use of food supplements since these are perceived to be safer. Here, we investigate the phytochemical profile and cholesterol-lowering potential of Protium heptaphyllum gum resin extract (PHE). Chemical characterization via HPLC-APCI-HRMS2 and…

0301 basic medicineModels MolecularProtein ConformationDrug Evaluation Preclinical030204 cardiovascular system & hematologyPharmacologyPPARαTerpenelcsh:ChemistryPCSK9chemistry.chemical_compound0302 clinical medicineCatalytic DomainSettore BIO/10 - BiochimicaPlant Gumslcsh:QH301-705.5SpectroscopyChromatography High Pressure LiquidFlame IonizationMonacolinChemistryAnticholesteremic AgentsGeneral MedicineComputer Science ApplicationsMolecular Docking SimulationCholesterolPhytochemicalMolecular dockinglipids (amino acids peptides and proteins)Breu brancoStatinmedicine.drug_classHypercholesterolemiaArticleCatalysisGas Chromatography-Mass SpectrometryInorganic Chemistry03 medical and health sciencesNutraceuticalmedicineHumansLovastatinPhysical and Theoretical ChemistryMolecular BiologyOleananeHMGCREnzymatic activityCholesterolPCSK9Organic ChemistryStatinSettore CHIM/08 - Chimica FarmaceuticaTriterpenes030104 developmental biologyhypercholesterolemia; gene expression; HMGCR; PCSK9; PPARα; enzymatic activity; molecular docking; statin; monacolin; breu brancolcsh:Biology (General)lcsh:QD1-999Breu branco; Enzymatic activity; Gene expression; HMGCR; Hypercholesterolemia; Molecular docking; Monacolin; PCSK9; PPARα; StatinLDL receptorDietary SupplementsHepatocytesSettore BIO/14 - FarmacologiaGene expressionHydroxymethylglutaryl-CoA Reductase InhibitorsResins PlantHydrogen
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Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages.

2016

We are thankful to the MAX-lab staff for their support during our visit at the synchrotron.; International audience; AP205 is a single-stranded RNA bacteriophage that has a coat protein sequence not similar to any other known single-stranded RNA phage. Here, we report an atomic-resolution model of the AP205 virus-like particle based on a crystal structure of an unassembled coat protein dimer and a cryo-electron microscopy reconstruction of the assembled particle, together with secondary structure information from site-specific solid-state NMR data. The AP205 coat protein dimer adopts the conserved Leviviridae coat protein fold except for the N-terminal region, which forms a beta-hairpin in …

0301 basic medicineModels MolecularRNA bacteriophageViral proteinCryo-electron microscopyProtein Conformation010402 general chemistrymedicine.disease_causeCrystallography X-Ray01 natural sciencesvirus-like particleBacteriophage03 medical and health sciencesStructural Biology[CHIM.ANAL]Chemical Sciences/Analytical chemistryLeviviridaemedicineRNA VirusesBacteriophages[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Molecular BiologyProtein secondary structurebiologyCryoelectron MicroscopyRNA[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologycircular permutationRNA PhagesCircular permutation in proteinsbiology.organism_classification3. Good health0104 chemical sciencesCrystallography030104 developmental biologycoat proteinBiophysicsLeviviridaeCapsid ProteinsJournal of molecular biology
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