Search results for " Mutation"

showing 10 items of 1212 documents

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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Identification of residues in the putative 5th helical region of human interleukin-6, important for activation of the IL-6 signal transducer, gp130

1996

AbstractWe have previously shown that L58 in the putative 5th helical region of human interleukin-6 (IL-6) is important for activation of the IL-6 signal transducer gp130 [de Hon et al. (1995) FEBS Lett. 369, 187–191]. To further explore the importance of individual residues in this region for gp130 activation we have now combined Ala substitutions of residues E52, S53, S54, K55, E56, L58 and E60 with other substitutions in IL-6, known to affect gp130 activation (Q160E and T163P). The combination mutant protein with L58A completely lost the capacity to induce the proliferation of XG-1 myeloma cells, and could effectively antagonize wild type IL-6 activity on these cells. Moreover, the data …

Models MolecularBiophysicsHuman Interleukin-6BiochemistryProtein Structure SecondaryStructure-function analysisgp130Signal Transducer gp130Antigens CDStructural BiologyMutant proteinCytokine Receptor gp130Escherichia coliTumor Cells CulturedGeneticsHumansPoint MutationCloning MolecularInterleukin 6Molecular BiologyAlanineMembrane GlycoproteinsbiologyInterleukin-6Wild typeCell BiologyGlycoprotein 130Recombinant ProteinsProtein Structure TertiaryCell biologyKineticsBiochemistryMutagenesis Site-Directedbiology.proteinLeukemia Erythroblastic AcuteMultiple MyelomaCell DivisionSignal TransductionFEBS Letters
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Recurrent Mutations in the Basic Domain of TWIST2 Cause Ablepharon Macrostomia and Barber-Say Syndromes

2015

Contains fulltext : 153827.pdf (Publisher’s version ) (Open Access) Ablepharon macrostomia syndrome (AMS) and Barber-Say syndrome (BSS) are rare congenital ectodermal dysplasias characterized by similar clinical features. To establish the genetic basis of AMS and BSS, we performed extensive clinical phenotyping, whole exome and candidate gene sequencing, and functional validations. We identified a recurrent de novo mutation in TWIST2 in seven independent AMS-affected families, as well as another recurrent de novo mutation affecting the same amino acid in ten independent BSS-affected families. Moreover, a genotype-phenotype correlation was observed, because the two syndromes differed based s…

Models MolecularCandidate geneHirsutismProtein ConformationHeLa Cellmedicine.disease_causeTranscriptomeTwist transcription factorModelsGenetics(clinical)ExomeEye AbnormalitiesNon-U.S. Gov'tExomeGenetics (clinical)ZebrafishGeneticsMutationMicroscopyMacrostomiaSetleis syndromeHypertelorismResearch Support Non-U.S. Gov'tHypertrichosiEyelid DiseaseGENÉTICAPhenotypeEyelid DiseasesAbnormalitiesMultipleSequence AnalysisHumanChromatin ImmunoprecipitationMolecular Sequence DataMutation MissenseHypertrichosisAbnormalities; Multiple; Amino Acid Sequence; Animals; Base Sequence; Chromatin Immunoprecipitation; Exome; Eye Abnormalities; Eyelid Diseases; HeLa Cells; Hirsutism; Humans; Hypertelorism; Hypertrichosis; Macrostomia; Microscopy; Electron; Molecular Sequence Data; Mutation; Missense; Protein Conformation; Repressor Proteins; Sequence Analysis; DNA; Skin Abnormalities; Twist Transcription Factor; Zebrafish; Models; Molecular; Phenotype; Genetics; Genetics (clinical)Other Research Radboud Institute for Molecular Life Sciences [Radboudumc 0]BiologyResearch SupportElectronArticleFrameshift mutationGeneticAblepharon macrostomia syndromeSkin AbnormalitieGeneticsmedicineJournal ArticleAnimalsHumansAbnormalities MultipleAmino Acid SequenceNeurodevelopmental disorders Donders Center for Medical Neuroscience [Radboudumc 7]Base SequenceAnimalTwist-Related Protein 1MolecularSequence Analysis DNADNARepressor Proteinmedicine.diseaseRepressor ProteinsTwist Transcription FactorEye AbnormalitieMicroscopy ElectronMutationSkin Abnormalitiessense organsMissenseNanomedicine Radboud Institute for Molecular Life Sciences [Radboudumc 19]HeLa CellsAmerican journal of human genetics
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Asp333, Asp495, and His52.3 Form the Catalytic Triad of Rat Soluble Epoxide Hydrolase

1996

On the basis of the sequence similarity between mammalian epoxide hydrolases and bacterial haloalkane dehalogenase reported earlier (Arand, M., Grant, D. F., Beetham, J. K., Friedberg, T., Oesch, F., and Hammock, B. D. (1994) FEBS Lett. 338, 251-256; Beetham, J. K., Grant, D., Arand, M., Garbarino, J., Kiyosue, T., Pinot, F., Oesch, F., Belknap, W. R., Shinozaki, K., and hammock, B. D. (1995) DNA Cell. Biol. 14, 61-71) we selected candidate amino acid residues for the putative catalytic triad of the rat soluble epoxide hydrolase. The predicted amino acid residues were exchanged by site-directed mutagenesis of the epoxide hydrolase cDNA, followed by the expression of the respective mutant en…

Models MolecularEpoxide hydrolase 2StereochemistryMolecular Sequence DataRestriction MappingPolymerase Chain ReactionBiochemistryCatalysisProtein Structure SecondaryCatalytic triadEscherichia coliAnimalsHumansPoint MutationHistidineAmino Acid SequenceCloning MolecularEpoxide hydrolaseMolecular BiologyPeptide sequenceDNA PrimersEpoxide Hydrolaseschemistry.chemical_classificationAspartic AcidBinding SitesSequence Homology Amino AcidChemistryCell BiologyRecombinant ProteinsRatsAmino acidEpoxide hydrolase activityKineticsBiochemistryEpoxide HydrolasesMutagenesis Site-DirectedHaloalkane dehalogenaseJournal of Biological Chemistry
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Gain-of-function mutations in IFIH1 cause a spectrum of human disease phenotypes associated with upregulated type I interferon signaling.

2014

The type I interferon system is integral to human antiviral immunity. However, inappropriate stimulation or defective negative regulation of this system can lead to inflammatory disease. We sought to determine the molecular basis of genetically uncharacterized cases of the type I interferonopathy Aicardi-Goutières syndrome, and of other patients with undefined neurological and immunological phenotypes also demonstrating an upregulated type I interferon response. We found that heterozygous mutations in the cytosolic double-stranded RNA receptor gene IFIH1 (MDA5) cause a spectrum of neuro-immunological features consistently associated with an enhanced interferon state. Cellular and biochemica…

Models MolecularInterferon-Induced Helicase IFIH1Molecular Sequence DataHDE NEU PEDElectrophoretic Mobility Shift AssayBiologymedicine.disease_causeNervous System MalformationsReal-Time Polymerase Chain ReactionArticleDEAD-box RNA HelicasesImmune systemAutoimmune Diseases of the Nervous SystemDownregulation and upregulationAnalysis of Variance; Autoimmune Diseases of the Nervous System; Base Sequence; DEAD-box RNA Helicases; Electrophoretic Mobility Shift Assay; Exome; HEK293 Cells; Humans; Interferon Type I; Microsatellite Repeats; Molecular Sequence Data; Mutation; Nervous System Malformations; Real-Time Polymerase Chain Reaction; Sequence Analysis DNA; Signal Transduction; Spectrum Analysis; Models Molecular; Phenotype; GeneticsModelsInterferonGeneticsmedicineHumansExomeMutationAnalysis of VarianceBase SequenceSpectrum AnalysisMolecularRNAMDA5DNASequence Analysis DNAMolecular biology3. Good healthInterferon Tipo IHEK293 CellsPhenotypeInterferon Type IMutationCancer researchSignal transductionSequence AnalysisInterferon type Imedicine.drugMicrosatellite RepeatsSignal TransductionNature genetics
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Missense variants in DPYSL5 cause a neurodevelopmental disorder with corpus callosum agenesis and cerebellar abnormalities

2021

International audience; The collapsin response mediator protein (CRMP) family proteins are intracellular mediators of neurotrophic factors regulating neurite structure/spine formation and are essential for dendrite patterning and directional axonal pathfinding during brain developmental processes. Among this family, CRMP5/DPYSL5 plays a significant role in neuronal migration, axonal guidance, dendrite outgrowth, and synapse formation by interacting with microtubules. Here, we report the identification of missense mutations in DPYSL5 in nine individuals with brain malformations, including corpus callosum agenesis and/or posterior fossa abnormalities, associated with variable degrees of intel…

Models MolecularMale0301 basic medicineHydrolases[SDV]Life Sciences [q-bio]Hippocampal formationMedical and Health Sciences0302 clinical medicineNeurodevelopmental disorderTubulinModelsNeurotrophic factorsCerebellumIntellectual disability2.1 Biological and endogenous factorsMissense mutationAetiologyChilddendrite branchingGenetics (clinical)de novo missense variantsPediatricGenetics & HeredityDPYSL5Biological Sciences[SDV] Life Sciences [q-bio]corpus callosum agenesisMental HealthChild PreschoolNeurologicalFemaleMicrotubule-Associated ProteinsAdultNeuriteIntellectual and Developmental Disabilities (IDD)primary neuronal culturesMutation MissenseBiologyYoung Adult03 medical and health sciencesRare DiseasesMediatorReportIntellectual DisabilityGeneticsmedicineHumansPreschoolCorpus Callosum Agenesisbrain malformationNeurosciencesMolecularmedicine.diseaseneurodevelopmental disorderBrain Disorders030104 developmental biologyNeurodevelopmental DisordersMutationMissenseAgenesis of Corpus CallosumNeuroscience030217 neurology & neurosurgery
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The Monod-Wyman-Changeux allosteric model accounts for the quaternary transition dynamics in wild type and a recombinant mutant human hemoglobin

2012

International audience; The acknowledged success of the Monod-Wyman-Changeux (MWC) allosteric model stems from its efficacy in accounting for the functional behavior of many complex proteins starting with hemoglobin (the paradigmatic case) and extending to channels and receptors. The kinetic aspects of the allosteric model, however, have been often neglected, with the exception of hemoglobin and a few other proteins where conformational relaxations can be triggered by a short and intense laser pulse, and monitored by time-resolved optical spectroscopy. Only recently the application of time-resolved wide-angle X-ray scattering (TR-WAXS), a direct structurally sensitive technique, unveiled th…

Models MolecularProtein ConformationcooperativityMESH: Catalytic DomainCooperativity01 natural sciencesMESH: Recombinant ProteinsHemoglobinsProtein structureMESH: Protein ConformationCatalytic Domainprotein structural dynamicsMESH: Allosteric Site0303 health sciencesMultidisciplinaryallosterybiologyMESH: KineticsChemistryBiological SciencesRecombinant Proteins[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsMESH: HemoglobinsAllosteric SiteMESH: Models MolecularAdultMESH: MutationStereochemistryKineticsAllosteric regulation010402 general chemistry03 medical and health sciencesprotein conformational changesflash photolysisallostery; cooperativity; flash photolysis; hemoglobin; protein conformational changes; protein structural dynamics; time-resolved wide angle x ray scattering; time-resolved x-ray scatteringHumans030304 developmental biologytime-resolved X-ray scattering; protein conformational changes; cooperativity; flash photolysisMESH: Humanstime-resolved X-ray scatteringWild typeActive sitetime-resolved wide angle x ray scatteringMESH: AdulthemoglobinSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)0104 chemical sciencesprotein conformational changeKineticsAllosteric enzymeMutationbiology.proteinHemoglobin
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Genomic determinants of protein folding thermodynamics in prokaryotic organisms.

2004

Here we investigate how thermodynamic properties of orthologous proteins are influenced by the genomic environment in which they evolve. We performed a comparative computational study of 21 protein families in 73 prokaryotic species and obtained the following main results. (i) Protein stability with respect to the unfolded state and with respect to misfolding are anticorrelated. There appears to be a trade-off between these two properties, which cannot be optimized simultaneously. (ii) Folding thermodynamic parameters are strongly correlated with two genomic features, genome size and G+C composition. In particular, the normalized energy gap, an indicator of folding efficiency in statistical…

Models MolecularProtein DenaturationProtein FoldingProtein familyArchaeal ProteinsThermodynamicsdeleterious mutationsthermophilic proteinsBiologymonte-carlo algorithmGenomeNegative selectionBacterial ProteinsStructural BiologyMolecular evolutionGenome ArchaealevolutionbuchneraMolecular BiologyGenome sizeGeneticsPrincipal Component Analysisacid side-chainsBacteriaSequence Homology Amino Acidreplica approachComputational BiologystabilityGenetic codeArchaeaPRI BioscienceFolding (chemistry)endosymbiotic bacteriacation-pi interactionsThermodynamicsProtein foldingHydrophobic and Hydrophilic InteractionsGenome BacterialJournal of molecular biology
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A human CCT5 gene mutation causing distal neuropathy impairs hexadecamer assembly in an archaeal model

2014

Chaperonins mediate protein folding in a cavity formed by multisubunit rings. The human CCT has eight non-identical subunits and the His147Arg mutation in one subunit, CCT5, causes neuropathy. Knowledge is scarce on the impact of this and other mutations upon the chaperone's structure and functions. To make progress, experimental models must be developed. We used an archaeal mutant homolog and demonstrated that the His147Arg mutant has impaired oligomeric assembly, ATPase activity, and defective protein homeostasis functions. These results establish for the first time that a human chaperonin gene defect can be reproduced and studied at the molecular level with an archaeal homolog. The major…

Models MolecularProtein FoldingProtein ConformationProtein subunitMutantMolecular Sequence Datahuman CCT5 gene mutation molecular dynamics neuropathy archaeal modelSequence alignmentGene mutationBiologyArticleChaperonin03 medical and health sciences0302 clinical medicineProtein structureHumansProtein Interaction Domains and MotifsAmino Acid Sequence030304 developmental biologyGenetics0303 health sciencesMultidisciplinarySettore BIO/16 - Anatomia UmanaArchaeaSettore CHIM/08 - Chimica FarmaceuticaChaperone (protein)Mutationbiology.proteinThermodynamicsProtein foldingProtein MultimerizationSequence Alignment030217 neurology & neurosurgeryChaperonin Containing TCP-1
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Identification of potential inhibitors targeting BRAF-V600E mutant melanoma cells.

2020

Models MolecularProto-Oncogene Proteins B-rafProtein ConformationMutantMutation MissenseDermatologyInhibitory Concentration 50Structure-Activity RelationshipCell Line TumormedicineHumansPoint MutationMolecular Targeted TherapyPrecision MedicineMelanomaProtein Kinase InhibitorsDose-Response Relationship Drugbusiness.industryMelanomaDrug Repositioningmedicine.diseaseNeoplasm ProteinsBRAF V600EMolecular Docking SimulationAmino Acid SubstitutionDrug DesignCancer researchIdentification (biology)Drug Screening Assays AntitumorbusinessJournal of the American Academy of Dermatology
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