Search results for "Protein Domains"

showing 10 items of 78 documents

De novo loss-of-function KCNMA1 variants are associated with a new multiple malformation syndrome and a broad spectrum of developmental and neurologi…

2019

Abstract KCNMA1 encodes the large-conductance Ca2+- and voltage-activated K+ (BK) potassium channel α-subunit, and pathogenic gain-of-function variants in this gene have been associated with a dominant form of generalized epilepsy and paroxysmal dyskinesia. Here, we genetically and functionally characterize eight novel loss-of-function (LoF) variants of KCNMA1. Genome or exome sequencing and the participation in the international Matchmaker Exchange effort allowed for the identification of novel KCNMA1 variants. Patch clamping was used to assess functionality of mutant BK channels. The KCNMA1 variants p.(Ser351Tyr), p.(Gly356Arg), p.(Gly375Arg), p.(Asn449fs) and p.(Ile663Val) abolished the …

MaleAtaxiaGenotypeDevelopmental DisabilitiesMutation MissenseBiology03 medical and health sciences0302 clinical medicineNeurodevelopmental disorderProtein DomainsLoss of Function MutationGeneticsmedicineHumansMissense mutationAbnormalities MultipleGenetic Predisposition to DiseaseProtein Interaction Domains and MotifsAlleleLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsMolecular BiologyAllelesGenetic Association StudiesGenetics (clinical)Loss functionExome sequencing030304 developmental biologyGenetics0303 health sciencesInfant NewbornGeneral MedicineParoxysmal dyskinesiamedicine.diseaseElectrophysiological PhenomenaPedigreePhenotypeAmino Acid SubstitutionSpeech delayFemaleGeneral Articlemedicine.symptom030217 neurology & neurosurgeryHuman Molecular Genetics
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Mutations in the Neuronal Vesicular SNARE VAMP2 Affect Synaptic Membrane Fusion and Impair Human Neurodevelopment

2019

VAMP2 encodes the vesicular SNARE protein VAMP2 (also called synaptobrevin-2). Together with its partners syntaxin-1A and synaptosomal-associated protein 25 (SNAP25), VAMP2 mediates fusion of synaptic vesicles to release neurotransmitters. VAMP2 is essential for vesicular exocytosis and activity-dependent neurotransmitter release. Here, we report five heterozygous de novo mutations in VAMP2 in unrelated individuals presenting with a neurodevelopmental disorder characterized by axial hypotonia (which had been present since birth), intellectual disability, and autistic features. In total, we identified two single-amino-acid deletions and three non-synonymous variants affecting conserved resid…

MaleHeterozygoteAdolescentVesicle-Associated Membrane Protein 2neuronal exocytosisynaptopathyautismsynaptobrevinMembrane FusionExocytosisR-SNARE ProteinsProtein DomainsReportIntellectual DisabilityGeneticsHumansAutistic DisorderChildGenetics (clinical)NeuronsNeurotransmitter Agentsneurodevelopmental disordersvesicle fusionBrainautism; epilepsy; movement disorders; neurodevelopmental disorders; neuronal exocytosis; SNARE; synaptobrevin; synaptopathy; VAMP2; vesicle fusionneuronal exocytosisLipidsMagnetic Resonance Imagingneurodevelopmental disorderautism epilepsy movement disorders neurodevelopmental disorders neuronal exocytosis SNARE synaptobrevin synaptopathy VAMP2 vesicle fusion Genetics Genetics (clinical)Phenotypeautism; epilepsy; movement disorders; neurodevelopmental disorders; neuronal exocytosis; SNARE; synaptobrevin; synaptopathy; VAMP2; vesicle fusion; Genetics; Genetics (clinical)VAMP2SNAREChild PreschoolMutationSynapsesMuscle Hypotoniaepilepsymovement disordersFemalesense organsmovement disorder
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A novel rat CVB1-VP1 monoclonal antibody 3A6 detects a broad range of enteroviruses

2018

AbstractEnteroviruses (EVs) are common RNA viruses that cause diseases ranging from rash to paralytic poliomyelitis. For example, EV-A and EV-C viruses cause hand-foot and mouth disease and EV-B viruses cause encephalitis and myocarditis, which can result in severe morbidity and mortality. While new vaccines and treatments for EVs are under development, methods for studying and diagnosing EV infections are still limited and therefore new diagnostic tools are required. Our aim was to produce and characterize new antibodies that work in multiple applications and detect EVs in tissues and in vitro. Rats were immunized with Coxsackievirus B1 capsid protein VP1 and hybridomas were produced. Hybr…

Models Molecular0301 basic medicineBiolääketieteet - BiomedicineProtein Conformationmedicine.drug_classImmunoelectron microscopylcsh:MedicineEnzyme-Linked Immunosorbent AssayCoxsackievirusmedicine.disease_causeMonoclonal antibodyenterovirusesArticleEpitopeEpitopesMice03 medical and health sciencesProtein DomainsEnterovirus InfectionsmedicineantibodiesAnimalsHumanslcsh:ScienceMultidisciplinary030102 biochemistry & molecular biologybiologyPolioviruslcsh:Rvasta-aineetAntibodies Monoclonalbiology.organism_classificationAntibodies NeutralizingImmunohistochemistryVirologyEnterovirus B HumanRats3. Good healthenterovirukset030104 developmental biologyKasvibiologia mikrobiologia virologia - Plant biology microbiology virologybiology.proteinImmunohistochemistrylcsh:QCapsid ProteinsAntibodyClone (B-cell biology)Protein BindingScientific Reports
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Targeting Cavity-Creating p53 Cancer Mutations with Small-Molecule Stabilizers: the Y220X Paradigm

2020

We have previously shown that the thermolabile, cavity-creating p53 cancer mutant Y220C can be reactivated by small-molecule stabilizers. In our ongoing efforts to unearth druggable variants of the p53 mutome, we have now analyzed the effects of other cancer-associated mutations at codon 220 on the structure, stability, and dynamics of the p53 DNA-binding domain (DBD). We found that the oncogenic Y220H, Y220N, and Y220S mutations are also highly destabilizing, suggesting that they are largely unfolded under physiological conditions. A high-resolution crystal structure of the Y220S mutant DBD revealed a mutation-induced surface crevice similar to that of Y220C, whereas the corresponding pock…

Models Molecular0301 basic medicineMutantCarbazolesDruggabilityCancer therapyAntineoplastic Agents01 natural sciencesBiochemistryDNA-binding proteinStructure-Activity Relationship03 medical and health sciencesProtein DomainsHumansCancer mutationsThermolabileQD0415Protein Stability010405 organic chemistryChemistryArticlesGeneral MedicineSmall moleculeAffinities0104 chemical sciences030104 developmental biologyGene Expression RegulationMutationBiophysicsMolecular MedicineMutant ProteinsDrug Screening Assays AntitumorTumor Suppressor Protein p53CrystallizationProtein BindingQD0241ACS Chemical Biology
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Molecular architecture and activation of the insecticidal protein Vip3Aa from Bacillus thuringiensis

2020

9 p.-5 fig.

Models Molecular0301 basic medicineProteasesBiologiaMolecular biologymedicine.medical_treatmentScienceAmino Acid MotifsBacillus thuringiensisGeneral Physics and Astronomy02 engineering and technologyGenetically modified cropsBiotecnologiaArticleProtein Structure SecondaryGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciencesBacterial ProteinsProtein DomainsTetramerBacillus thuringiensisElectron microscopymedicineTrypsinlcsh:ScienceMultidisciplinaryProteasebiologyChemistryQfungifood and beveragesMidgutGeneral Chemistry021001 nanoscience & nanotechnologybiology.organism_classification030104 developmental biologyStructural biologyBiochemistrylcsh:QStructural biology0210 nano-technologyProteïnesFunction (biology)
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High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain

2020

AbstractDuring storage in the silk gland, the N-terminal domain (NT) of spider silk proteins (spidroins) keeps the aggregation-prone repetitive region in solution at extreme concentrations. We observe that NTs from different spidroins have co-evolved with their respective repeat region, and now use an NT that is distantly related to previously used NTs, for efficient recombinant production of the amyloid-β peptide (Aβ) implicated in Alzheimer’s disease. A designed variant of NT from Nephila clavipes flagelliform spidroin, which in nature allows production and storage of β-hairpin repeat segments, gives exceptionally high yields of different human Aβ variants as a solubility tag. This tool e…

Models Molecular0301 basic medicineProtein domainBiophysicslcsh:MedicinePeptideBiosynthesis010402 general chemistryBiochemistry01 natural sciencesArticlelaw.invention03 medical and health sciencesProtein DomainslawAnimalsSpider silkAmino Acid SequenceNeurodegenerationlcsh:SciencePeptide sequencechemistry.chemical_classificationAmyloid beta-PeptidesMultidisciplinarybiologySpidroinlcsh:RNeurodegenerative diseasesNephila clavipesProteinsbiology.organism_classification0104 chemical sciences030104 developmental biologyBiochemistrychemistryYield (chemistry)Recombinant DNAlcsh:QPeptidesFibroinsScientific Reports
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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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Modulation of Structural Heterogeneity Controls Phytochrome Photoswitching

2019

Phytochromes sense red/far-red light and control many biological processes in plants, fungi, and bacteria. Although crystal structures of dark and light adapted states have been determined, the molecular mechanisms underlying photoactivation remains elusive. Here we demonstrate that the conserved tongue region of the PHY domain of a 57kDa photosensory module of Deinococcus radiodurans phytochrome, changes from a structurally heterogeneous dark state to an ordered light activated state. The results were obtained in solution by utilizing a laser-triggered activation approach detected on the atomic level with high-resolution protein NMR spectroscopy. The data suggest that photosignaling of phy…

Models MolecularLightTongue regionBiophysicsphototransduction03 medical and health sciences0302 clinical medicineProtein DomainsPHYmolekyylidynamiikkaprotein structureNMR-spektroskopiaNuclear Magnetic Resonance Biomolecular030304 developmental biologyphytochrome0303 health sciencesPhytochromebiologyChemistryProtein NMR SpectroscopyDeinococcus radioduransArticlesDarknessbiology.organism_classificationmolecular dynamicsNMRStructural heterogeneityDark stateModulationBiophysicsvalokemiaproteiinitDeinococcusPhytochrome030217 neurology & neurosurgeryBiophysical Journal
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Revisiting the cysteine-rich proteins encoded in the 3’-proximal open reading frame of the positive-sense single-stranded RNA of some monopartite fil…

2020

A reexamination of proteins with conserved cysteines and basic amino acids encoded by the 3 '-proximal gene of the positive-sense single-stranded RNA of some monopartite filamentous plant viruses has been carried out. The cysteines are involved in a putative Zn-finger domain, which, together with the basic amino acids, form part of the nuclear or nucleolar localization signals. An in-depth study of one of these proteins, p15 from grapevine B virus (GVB), has shown: (i) a three-dimensional structure with four alpha-helices predicted by two independent in silico approaches, (ii) the nucleolus as the main accumulation site by applying confocal laser microscopy to a fusion between p15 and the g…

Models MolecularProtein Conformation alpha-HelicalGrapevine virus BAgroinfiltrationEvolutionProtein ConformationProtein DomainProtein domainNicotiana benthamianaGene ExpressionBiologyEvolution MolecularOpen Reading Frames03 medical and health sciencesViral ProteinsProtein DomainsPlant CellsVirologyTobaccoGene expressionAmino Acid SequenceCloning MolecularGenePhylogeny030304 developmental biologyGenetics0303 health sciencesSequence Homology Amino Acid030306 microbiologyRNASettore AGR/12 - Patologia VegetaleGeneral Medicinebiology.organism_classificationVirologyRecombinant ProteinsPlant LeavesRNA silencingRNA ViralFlexiviridaeSequence AlignmentModel
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Characterization of the pleiotropic LysR-type transcription regulator LeuO of Escherichia coli

2019

AbstractLeuO is a pleiotropic LysR-type transcriptional regulator (LTTR) and co-regulator of the abundant nucleoid-associated repressor protein H-NS in Gammaproteobacteria. As other LTTRs, LeuO is a tetramer that is formed by dimerization of the N-terminal DNA-binding domain (DBD) and C-terminal effector-binding domain (EBD). To characterize the Escherichia coli LeuO protein, we screened for LeuO mutants that activate the cas (CRISPR-associated/Cascade) promoter more effectively than wild-type LeuO. This yielded nine mutants carrying amino acid substitutions in the dimerization interface of the regulatory EBD, as shown by solving the EBD’s crystal structure. Superimposing of the crystal str…

Models MolecularProtein domainMutantRepressorPlasma protein bindingBiologymedicine.disease_cause03 medical and health sciencesProtein DomainsTranscription (biology)GeneticsConsensus sequencemedicinePromoter Regions GeneticEscherichia coli030304 developmental biologyGenetics0303 health sciences030306 microbiologyEscherichia coli ProteinsGene regulation Chromatin and EpigeneticsGenetic PleiotropyDNAGene Expression Regulation BacterialDNA-Binding ProteinsMutationNucleic Acid ConformationProtein MultimerizationDeoxyribonuclease IProtein BindingTranscription FactorsNucleic Acids Research
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