Search results for "DOMAIN"

showing 10 items of 2485 documents

Diverse relations between ABC transporters and lipids: An overview.

2016

It was first discovered in 1992 that P-glycoprotein (Pgp, ABCB1), an ATP binding cassette (ABC) transporter, can transport phospholipids such as phosphatidylcholine, -ethanolamine and -serine as well as glucosylceramide and glycosphingolipids. Subsequently, many other ABC transporters were identified to act as lipid transporters. For substrate transport by ABC transporters, typically a classic, alternating access model with an ATP-dependent conformational switch between a high and a low affinity substrate binding site is evoked. Transport of small hydrophilic substrates can easily be imagined this way, as the molecule can in principle enter and exit the transporter in the same orientation. …

0301 basic medicineModels MolecularATP Binding Cassette Transporter Subfamily BBiophysicsGene ExpressionATP-binding cassette transporterPhosphatidylserinesBiologyBiochemistrySubstrate SpecificitySerine03 medical and health sciencesLipid translocationHumansProtein IsoformsBinding siteLipid bilayerLipid TransportATP-binding domain of ABC transportersBinding SitesPhosphatidylethanolaminesFatty AcidsTransporterBiological TransportCell BiologyCell biology030104 developmental biologyBiochemistryPhosphatidylcholineslipids (amino acids peptides and proteins)Protein BindingBiochimica et biophysica acta. Biomembranes
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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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Biological insertion of computationally designed short transmembrane segments

2016

The great majority of helical membrane proteins are inserted co-translationally into the ER membrane through a continuous ribosome-translocon channel. The efficiency of membrane insertion depends on transmembrane (TM) helix amino acid composition, the helix length and the position of the amino acids within the helix. In this work, we conducted a computational analysis of the composition and location of amino acids in transmembrane helices found in membrane proteins of known structure to obtain an extensive set of designed polypeptide segments with naturally occurring amino acid distributions. Then, using an in vitro translation system in the presence of biological membranes, we experimental…

0301 basic medicineModels MolecularBiologyEndoplasmic ReticulumArticleProtein Structure Secondary03 medical and health sciencesOrientations of Proteins in Membranes databaseMembranes (Biologia)Amino Acid SequenceIntegral membrane proteinMultidisciplinary030102 biochemistry & molecular biologyPeripheral membrane proteinCell MembraneProteïnes de membranaComputational BiologyMembrane ProteinsBiological membraneBiofísicaTransmembrane proteinTransmembrane domain030104 developmental biologyBiochemistryMembrane proteinHelixBiophysicsPeptidesScientific Reports
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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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Sensory domain contraction in histidine kinase CitA triggers transmembrane signaling in the membrane-bound sensor

2017

Bacteria use membrane-integral sensor histidine kinases (HK) to perceive stimuli and transduce signals from the environment to the cytosol. Information on how the signal is transmitted across the membrane by HKs is still scarce. Combining both liquid- and solid-state NMR, we demonstrate that structural rearrangements in the extracytoplasmic, citrate-sensing Per-Arnt-Sim (PAS) domain of HK CitA are identical for the isolated domain in solution and in a longer construct containing the membrane-embedded HK and lacking only the kinase core. We show that upon citrate binding, the PAS domain contracts, resulting in a shortening of the C-terminal β-strand. We demonstrate that this contraction of t…

0301 basic medicineModels MolecularHistidine Kinase030106 microbiologyMolecular ConformationCitric Acid03 medical and health sciencesStructure-Activity RelationshipBacterial ProteinsPAS domainProtein Interaction Domains and MotifsAmino Acid SequenceHistidineMultidisciplinaryChemistryKinaseHistidine kinaseGeobacillusMembrane ProteinsBiological SciencesTransmembrane proteinCell biologyCytosolHelixSignal transductionProtein BindingSignal Transduction
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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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Evolving Notch polyQ tracts reveal possible solenoid interference elements.

2016

ABSTRACTPolyglutamine (polyQ) tracts in regulatory proteins are extremely polymorphic. As functional elements under selection for length, triplet repeats are prone to DNA replication slippage and indel mutations. Many polyQ tracts are also embedded within intrinsically disordered domains, which are less constrained, fast evolving, and difficult to characterize. To identify structural principles underlying polyQ tracts in disordered regulatory domains, here I analyze deep evolution of metazoan Notch polyQ tracts, which can generate alleles causing developmental and neurogenic defects. I show that Notch features polyQ tract turnover that is restricted to a discrete number of conserved “polyQ …

0301 basic medicineModels MolecularProtein Structure ComparisonProtein FoldingHuntingtinlcsh:MedicineCarboxamideAnkyrin Repeat DomainBiochemistryProtein Structure SecondaryDatabase and Informatics Methods0302 clinical medicineProtein structureMacromolecular Structure AnalysisDrosophila Proteinslcsh:ScienceGeneticsHuntingtin ProteinMultidisciplinaryReceptors NotchChemistryDrosophila MelanogasterAnimal ModelsCell biologyInsectsExperimental Organism SystemsProtein foldingDrosophilaSequence AnalysisResearch ArticleMultiple Alignment CalculationProtein StructureArthropodamedicine.drug_classBioinformaticsProtein domainSequence alignmentBiologyIntrinsically disordered proteinsResearch and Analysis MethodsTerminal loopEvolution Molecular03 medical and health sciencesModel OrganismsProtein DomainsSequence Motif AnalysisComputational TechniquesmedicineHuntingtin ProteinAnimalsIndelMolecular BiologyRepetitive Sequences Nucleic AcidModels GeneticSequence Homology Amino Acidlcsh:RDNA replicationOrganismsBiology and Life SciencesProteinsHydrogen BondingInvertebratesSplit-Decomposition MethodIntrinsically Disordered Proteins030104 developmental biologyAnkyrin repeatlcsh:QPeptidesSequence Alignment030217 neurology & neurosurgeryPLoS ONE
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Conformational dynamism for DNA interaction in the Salmonella RcsB response regulator

2017

17 páginas, 7 figuras, 1 tabla

0301 basic medicineModels MolecularSalmonella typhimuriumProtein Data Bank (RCSB PDB)Plasma protein bindingBiologyCrystallography X-RayDNA-binding protein03 medical and health sciencesBacterial ProteinsProtein DomainsStructural BiologyGeneticsAmino Acid SequencePhosphorylationTranscription factorSequence Homology Amino AcidEffectorPromoterDNACell biologyResponse regulator030104 developmental biologyRegulonBiochemistryNucleic Acid ConformationProtein BindingNucleic Acids Research
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