Search results for "DOMAIN"

showing 10 items of 2485 documents

Structure of the Human TRPML2 Ion Channel Extracytosolic/Lumenal Domain.

2019

Summary TRPML2 is the least structurally characterized mammalian transient receptor potential mucolipin ion channel. The TRPML family hallmark is a large extracytosolic/lumenal domain (ELD) between transmembrane helices S1 and S2. We present crystal structures of the tetrameric human TRPML2 ELD at pH 6.5 (2.0 A) and 4.5 (2.95 A), corresponding to the pH values in recycling endosomes and lysosomes. Isothermal titration calorimetry shows Ca2+ binding to the highly acidic central pre-pore loop which is abrogated at low pH, in line with a pH-dependent channel regulation model. Small angle X-ray scattering confirms the ELD dimensions in solution. Changes in pH or Ca2+ concentration do not affect…

Models Molecular0303 health sciencesBinding SitesTRPMLEndosomeChemistrySmall-angle X-ray scatteringProtein Conformation030302 biochemistry & molecular biologyIsothermal titration calorimetryHydrogen-Ion ConcentrationCrystallography X-Ray03 medical and health sciencesTransient receptor potential channelTransmembrane domainTransient Receptor Potential ChannelsProtein DomainsStructural BiologyBiophysicsHumansCalciumMolecular BiologyProtein secondary structureIon channel030304 developmental biologyStructure (London, England : 1993)
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Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site

2003

Epoxide hydrolases are essential for the processing of epoxide-containing compounds in detoxification or metabolism. The classic epoxide hydrolases have an alpha/beta hydrolase fold and act via a two-step reaction mechanism including an enzyme-substrate intermediate. We report here the structure of the limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis, solved using single-wavelength anomalous dispersion from a selenomethionine-substituted protein and refined at 1.2 A resolution. This enzyme represents a completely different structure and a novel one-step mechanism. The fold features a highly curved six-stranded mixed beta-sheet, with four alpha-helices packed onto it to create a …

Models MolecularAFSG Stafafdelingen (WUATV)10050 Institute of Pharmacology and Toxicologydrug protein bindingEnantioselectivityEpoxide hydrolaseCrystallography X-Rayuncultured actinomyceteCatalytic Domain2400 General Immunology and Microbiologyalpha helixRhodococcuscholesterol epoxide hydrolasenaphthalene 12-dioxygenasedcl14limonene 12 epoxide hydrolaseEpoxide hydrolaseBacteria (microorganisms)delta(5)-3-ketosteroid isomeraseEpoxide HydrolasesLimonene-12-epoxide hydrolaseGeneral Neurosciencearticle2800 General NeuroscienceActinobacteria (class)Articlesagrobacterium-radiobacterEnzyme structureRecombinant Proteinsunclassified drugenzyme structurereaction analysisBiochemistrypriority journalenzyme active siteMechanism2-dioxygenaseDimerizationBiotechnologychemical reactioncrystal structureaspergillus-nigermacromolecular structuresStereochemistrybeta sheetvalpromideMolecular Sequence Data610 Medicine & healthGenetics and Molecular BiologyBiologyGeneral Biochemistry Genetics and Molecular BiologyBacterial Proteinssite directed mutagenesis1300 General Biochemistry Genetics and Molecular BiologyHydrolase1312 Molecular BiologyAmino Acid SequencedetoxificationRhodococcus erythropolisBiologyMonoterpene degradationMolecular Biologyprotein data-bankenzyme substrate complexEnzyme substrate complexnonhumancatalysisSequence Homology Amino AcidGeneral Immunology and Microbiologybacterial enzymeActive sitecrystal-structureAFSG Staff Departments (WUATV)enzyme metabolismProtein SubunitsenzymeEpoxide HydrolasesGeneral Biochemistrybiology.proteinMutagenesis Site-Directed570 Life sciences; biologyselenomethioninenaphthalene 1Alpha helix
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Determination of enrichment factors for modified RNA in MeRIP experiments

2019

In the growing field of RNA modification, precipitation techniques using antibodies play an important role. However, little is known about their specificities and protocols are missing to assess their effectiveness. Here we present a method to assess enrichment factors after MeRIP-type pulldown experiments, here exemplified with a commercial antibody against N6-methyladenosine (m6A). Testing different pulldown and elution conditions, we measure enrichment factors of 4-5 using m6A-containing mRNAs against an unmodified control of identical sequence. Both types of mRNA carry 32P labels at different nucleotides, allowing their relative quantification in a mixture after digestion to nucleotides…

Models MolecularAdenosineAbsolute quantificationMethylationProtein Structure SecondaryGeneral Biochemistry Genetics and Molecular BiologyViral Proteins03 medical and health sciencesAdenosine TriphosphateRNA modificationEscherichia coliHumansImmunoprecipitationProtein Interaction Domains and MotifsNucleotideRNA MessengerMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesMessenger RNACell-Free SystemChemistryElution030302 biochemistry & molecular biologyRNADNA-Directed RNA PolymerasesBiochemistryImmunoglobulin GIsotope LabelingChromatography Thin LayerPhosphorus RadioisotopesProtein BindingMethods
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Investigation of new 2-aryl substituted Benzothiopyrano[4,3-d[pyrimidines as kinase inhibitors targeting vascular endothelial growth factor receptor 2

2015

Vascular Endothelial Growth Factor (VEGF) pathway has emerged as one of the most important positive modulators of Angiogenesis, a central process implicated in tumour growth and metastatic dissemination. This led to the design and development of anti-VEGF monoclonal antibodies and small-molecule ATP-competitive VEGFR-inhibitors. In this study, we describe the synthesis and the biological evaluation of novel 2-aryl substituted benzothiopyrano-fused pyrimidines 1a-i, 2a-i and 3a-i. The ability of the compounds to target the VEGF pathway was determined in vitro exploiting the compounds' antiproliferative efficacy against HUVEC cells. The VEGFR-2 inhibition was confirmed by enzymatic assays on …

Models MolecularAngiogenesisReceptor tyrosine kinaseCellAntineoplastic AgentsReceptor tyrosine kinaseBenzothiopyranopirimidines; Kinase inhibitors; Receptor tyrosine kinases; Tumor angiogenesis; VEGFR;Tumor angiogenesisStructure-Activity Relationshipchemistry.chemical_compoundVEGFRBenzothiopyranopirimidineCell Line TumorReceptor tyrosine kinasesDrug DiscoveryHuman Umbilical Vein Endothelial CellsmedicineHumansProtein Kinase InhibitorsCell ProliferationPyransTumor angiogenesiPharmacologyKinase inhibitorDose-Response Relationship DrugMolecular StructurebiologyKinaseCell growthOrganic ChemistryKinase insert domain receptorGeneral MedicineVascular Endothelial Growth Factor Receptor-2Molecular biologyVascular endothelial growth factorPyrimidinesmedicine.anatomical_structureBenzothiopyranopirimidineschemistryBenzothiopyranopirimidines; Kinase inhibitors; Receptor tyrosine kinases; Tumor angiogenesis; VEGFRKinase inhibitorsCancer researchbiology.proteinDrug Screening Assays AntitumorEx vivo
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Charge Pair Interactions in Transmembrane Helices and Turn Propensity of the Connecting Sequence Promote Helical Hairpin Insertion

2013

alpha-Helical hairpins, consisting of a pair of closely spaced transmembrane (TM) helices that are connected by a short interfacial turn, are the simplest structural motifs found in multi-spanning membrane proteins. In naturally occurring hairpins, the presence of polar residues is common and predicted to complicate membrane insertion. We postulate that the pre-packing process offsets any energetic cost of allocating polar and charged residues within the hydrophobic environment of biological membranes. Consistent with this idea, we provide here experimental evidence demonstrating that helical hairpin insertion into biological membranes can be driven by electrostatic interactions between clo…

Models MolecularBioquímicaProtein FoldingGlycosylationMolecular Sequence Datamembrane integrationEndoplasmic Reticulumsalt bridgeProtein Structure SecondaryTurn (biochemistry)Viral Proteins03 medical and health sciencesProtein structureStructural BiologyComputer SimulationAmino Acid SequenceAmino AcidsStructural motifMolecular Biologytranslocon030304 developmental biology0303 health sciencesBinding SitesChemistry030302 biochemistry & molecular biologyProteïnes de membranaBiochemistry and Molecular BiologyMembrane ProteinsBiological membraneTransloconelectrostatic interactionsTransmembrane proteinProtein Structure TertiaryPoliovirusProtein TransportCrystallographyTransmembrane domainhelical hairpinMembrane proteinMutationBiophysicsElectrophoresis Polyacrylamide GelHydrophobic and Hydrophilic InteractionsBiokemi och molekylärbiologi
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Tetravalent single-chain avidin: from subunits to protein domains via circularly permuted avidins

2005

scAvd (single-chain avidin, where two dcAvd are joined in a single polypeptide chain), having four biotin-binding domains, was constructed by fusion of topologically modified avidin units. scAvd showed similar biotin binding and thermal stability properties as chicken avidin. The DNA construct encoding scAvd contains four circularly permuted avidin domains, plus short linkers connecting the four domains into a single polypeptide chain. In contrast with wild-type avidin, which contains four identical avidin monomers, scAvd enables each one of the four avidin domains to be independently modified by protein engineering. Therefore the scAvd scaffold can be used to construct spatially and stoich…

Models MolecularBiotin bindingProtein domainMolecular Sequence DataProtein EngineeringBiochemistrychemistry.chemical_compoundMoleculeAnimalsMolecular BiologyCells CulturedBinding SitesbiologyChemistryCell BiologyProtein engineeringCircular permutation in proteinsAvidinProtein Structure TertiaryCrystallographyProtein SubunitsMonomerBiophysicsbiology.proteinDNA constructChickensAvidinResearch ArticleProtein Binding
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Picomolar inhibition of cholera toxin by a pentavalent ganglioside GM1os-calix[5]arene

2013

Cholera toxin (CT), the causative agent of cholera, displays a pentavalent binding domain that targets the oligosaccharide of ganglioside GM1 (GM1os) on the periphery of human abdominal epithelial cells. Here, we report the first GM1os-based CT inhibitor that matches the valency of the CT binding domain (CTB). This pentavalent inhibitor contains five GM1os moieties linked to a calix[5]arene scaffold. When evaluated by an inhibition assay, it achieved a picomolar inhibition potency (IC50 = 450 pM) for CTB. This represents a significant multivalency effect, with a relative inhibitory potency of 100000 compared to a monovalent GM1os derivative, making GM1os-calix[5]arene one of the most potent…

Models MolecularCholera ToxinbindingStereochemistrydesignCalix[5]areneEpithelial cellsG(M1) GangliosideHeat-labile enterotoxinmedicine.disease_causeligandBiochemistrycrystalMultivalency effectsCholeraCausative agentsmedicinePotencyHumansoligosaccharidePhysical and Theoretical ChemistryIC50Vibrio choleraeheat-labile enterotoxinVLAGchemistry.chemical_classificationgm1 mimicsGangliosideInhibition assaysChemistryCholera toxinOrganic ChemistryOligosaccharideBinding domainLigand (biochemistry)ValenciesOrganische ChemiehexamethylenetetramineChemistryPositive ionsaffinityAntitoxinsCalixarenesrecognitionBinding domain
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Critical Role of Substrate Conformational Change in the Proton Transfer Process Catalyzed by 4-Oxalocrotonate Tautomerase

2009

4-Oxalocrotonate tautomerase enzyme (4-OT) catalyzes the isomerization of 2-oxo-4-hexenedioate to 2-oxo-3-hexenedioate. The chemical process involves two proton transfers, one from a carbon of the substrate to the nitrogen of Pro1 and another from this nitrogen atom to a different carbon of the substrate. In this paper the isomerization has been studied using the combined quantum mechanical and molecular mechanical (QM/MM) method with a dual-level treatment of the quantum subsystem employing the MPW1BK density functional as the higher level. Exploration of the potential energy surface shows that the process is stepwise, with a stable intermediate state corresponding to the deprotonated subs…

Models MolecularConformational changeProtonMolecular ConformationProtonationCrystallography X-RayBiochemistryArticleCatalysisColloid and Surface ChemistryReaction rate constantIsomerismCatalytic DomainIsomerasesChemistrySubstrate (chemistry)Hydrogen BondingGeneral ChemistryChemical physicsCrotonatesPotential energy surface4-Oxalocrotonate tautomeraseQuantum TheoryThermodynamicsPhysical chemistryProtonsIsomerizationJournal of the American Chemical Society
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Plasticity of the PAS domain and a potential role for signal transduction in the histidine kinase DcuS

2008

The mechanistic understanding of how membrane-embedded sensor kinases recognize signals and regulate kinase activity is currently limited. Here we report structure-function relationships of the multidomain membrane sensor kinase DcuS using solid-state NMR, structural modeling and mutagenesis. Experimental data of an individual cytoplasmic Per-Arnt-Sim (PAS) domain were compared to structural models generated in silico. These studies, together with previous NMR work on the periplasmic PAS domain, enabled structural investigations of a membrane-embedded 40-kDa construct by solid-state NMR, comprising both PAS segments and the membrane domain. Structural alterations are largely limited to prot…

Models MolecularCytoplasmHistidine KinaseMolecular Sequence DataHAMP domainStructural BiologyPAS domainEscherichia coliAmino Acid SequenceKinase activityProtein Structure QuaternaryNuclear Magnetic Resonance BiomolecularMolecular BiologybiologyEscherichia coli ProteinsHistidine kinaseProtein Structure TertiaryCell biologyTransmembrane domainBiochemistryProtein kinase domainCyclic nucleotide-binding domainbiology.proteinGRB2Protein KinasesSignal Transduction
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Flexible Structure of Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21.

2015

Filamins (FLNs) are large, multidomain actin cross-linking proteins with diverse functions. Besides regulating the actin cytoskeleton, they serve as important links between the extracellular matrix and the cytoskeleton by binding cell surface receptors, functioning as scaffolds for signaling proteins, and binding several other cytoskeletal proteins that regulate cell adhesion dynamics. Structurally, FLNs are formed of an amino terminal actin-binding domain followed by 24 immunoglobulin-like domains (IgFLNs). Recent studies have demonstrated that myosin-mediated contractile forces can reveal hidden protein binding sites in the domain pairs IgFLNa18-19 and 20-21, enabling FLNs to transduce me…

Models MolecularDIMERIZATIONMagnetic Resonance SpectroscopyFilaminsProtein domainlcsh:MedicinePlasma protein bindingmacromolecular substancesBiologyMyosinsFilaminCrystallography X-RayLigandsfilaminsFORCEProtein structureAUTO-INHIBITIONBINDINGEscherichia coliCytoskeletonPHOSPHORYLATIONlcsh:ScienceCytoskeletonFRAGMENTMultidisciplinaryBinding Siteslcsh:Rta1182Signal transducing adaptor proteinfilamiinitSMALL-ANGLE SCATTERINGActin cytoskeletonActinsRecombinant ProteinsCell biologyProtein Structure TertiaryMODELBIOLOGICAL MACROMOLECULESCytoskeletal Proteinspeptiditpeptides1182 Biochemistry cell and molecular biologylcsh:QPeptidesINTEGRINBinding domainProtein BindingResearch ArticlePloS one
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