Search results for "Protein Domains"

showing 10 items of 78 documents

What monomeric nucleotide binding domains can teach us about dimeric ABC proteins

2020

The classic conceptualization of ATP binding cassette (ABC) transporter function is an ATP-dependent conformational change coupled to transport of a substrate across a biological membrane via the transmembrane domains (TMDs). The binding of two ATP molecules within the transporter's two nucleotide binding domains (NBDs) induces their dimerization. Despite retaining the ability to bind nucleotides, isolated NBDs frequently fail to dimerize. ABC proteins without a TMD, for example ABCE and ABCF, have NBDs tethered via elaborate linkers, further supporting that NBD dimerization does not readily occur for isolated NBDs. Intriguingly, even in full-length transporters, the NBD-dimerized, outward-…

Conformational changeBiophysicsContext (language use)ATP-binding cassette transporterBiochemistry03 medical and health sciencesAdenosine TriphosphateProtein DomainsStructural BiologyGeneticsAnimalsHumansNucleotideMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesBinding Sites030302 biochemistry & molecular biologyTransporterBiological membraneCell BiologyTransmembrane domainchemistryCyclic nucleotide-binding domainBiophysicsATP-Binding Cassette Transporterslipids (amino acids peptides and proteins)Protein MultimerizationProtein BindingFEBS Letters
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Deinococcus radiodurans' SRA-HNH domain containing protein Shp (Dr1533) is involved in faithful genome inheritance maintenance following DNA damage

2018

WOS:000452343100012; International audience; Background: Deinococcus radiodurans R1 (DR) survives conditions of extreme desiccation, irradiation and exposure to genotoxic chemicals, due to efficient DNA breaks repair, also through Mn2+ protection of DNA repair enzymes. Methods: Possible annotated domains of the DR1533 locus protein (Shp) were searched by bioinformatic analysis. The gene was cloned and expressed as fusion protein. Band-shift assays of Shp or the SRA and HNH domains were performed on oligonucleotides, genomic DNA from E. coif and DR. slip knock-out mutant was generated by homologous recombination with a kanamycin resistance cassette. Results: DR1533 contains an N-terminal SRA…

DNA RepairDNA cytosine-methylation; DNA damage; DR1533 locus; Genotoxic agents; Mn2+; SRA domain; Biophysics; Biochemistry; Molecular BiologyGenotoxic agents[SDV]Life Sciences [q-bio]DNA cytosine-methylationperspectiveSettore BIO/19 - Microbiologia GeneraleBiochemistrychemistry.chemical_compound0302 clinical medicineKanamycinCloning Molecularcytosine0303 health sciencesDR1533 locusbiologyChemistryGenotoxic agentuhrf1Mn(2+)Mn2+SRA domainDeinococcusrecognitionmanganese(ii)DNA BacterialDNA damageDNA repairoxidationUbiquitin-Protein LigasesBiophysicsSettore BIO/11 - Biologia Molecolareresistance03 medical and health sciencesBacterial ProteinsProtein DomainsDR1533 locuDrug Resistance BacterialEscherichia coliHumansfeaturesAmino Acid SequenceGeneMolecular Biology030304 developmental biologyOligonucleotideComputational BiologyDeinococcus radioduransDNA Methylationbiology.organism_classificationMolecular biologygenomic DNArepairMutationCCAAT-Enhancer-Binding ProteinsDNA damageHomologous recombination030217 neurology & neurosurgeryDNAGenome BacterialMutagens
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Microscopic interactions between ivermectin and key human and viral proteins involved in SARS-CoV-2 infection

2021

The identification of chemical compounds able to bind specific sites of the human/viral proteins involved in the SARS-CoV-2 infection cycle is a prerequisite to design effective antiviral drugs. Here we conduct a molecular dynamics study with the aim to assess the interactions of ivermectin, an antiparasitic drug with broad-spectrum antiviral activity, with the human Angiotensin-Converting Enzyme 2 (ACE2), the viral 3CLpro and PLpro proteases, and the viral SARS Unique Domain (SUD). The drug/target interactions have been characterized in silico by describing the nature of the non-covalent interactions found and by measuring the extent of their time duration along the MD simulation. Results …

DrugProteasesIn silicomedia_common.quotation_subjectProtein domainCoronavirus Papain-Like ProteasesGeneral Physics and AstronomyPlasma protein bindingBiologyAntiviral AgentsivermectinProtein DomainsMolecular dynamics simulationHumansPhysical and Theoretical ChemistryBinding siteCoronavirus 3C Proteasesmedia_commonchemistry.chemical_classificationSARS Unique DomainBinding SitesSARS-CoV-2SARS-CoV-2 infectionRNAHydrogen BondingVirologyG-QuadruplexesMolecular Docking SimulationEnzymechemistrySettore CHIM/03 - Chimica Generale E InorganicaRNAAngiotensin-Converting Enzyme 2Hydrophobic and Hydrophilic InteractionsProtein BindingPhysical Chemistry Chemical Physics
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Identification of the essential protein domains for Mib2 function during the development of the Drosophila larval musculature and adult flight muscles

2016

The proper differentiation and maintenance of myofibers is fundamental to a functional musculature. Disruption of numerous mostly structural factors leads to perturbations of these processes. Among the limited number of known regulatory factors for these processes is Mind bomb2 (Mib2), a muscle-associated E3 ubiquitin ligase, which was previously established to be required for maintaining the integrity of larval muscles. In this study, we have examined the mechanistic aspects of Mib2 function by performing a detailed functional dissection of the Mib2 protein. We show that the ankyrin repeats, in its entirety, and the hitherto uncharacterized Mib-specific domains (MIB), are important for the…

EmbryologyLife CyclesMuscle PhysiologyMuscle FunctionsPhysiologylcsh:MedicineMuscle ProteinsAnkyrin Repeat DomainMuscle DevelopmentBiochemistryAnimals Genetically ModifiedMedicine and Health SciencesDrosophila Proteinslcsh:ScienceMusculoskeletal SystemAbdominal MusclesMusclesDrosophila MelanogasterMetamorphosis BiologicalPupaAnimal ModelsNaturwissenschaftliche FakultätAnkyrin RepeatInsectsExperimental Organism SystemsLarvaDrosophilaAnatomyResearch ArticleArthropoda-Research and Analysis MethodsModel OrganismsProtein Domainsddc:570GeneticsAnimalsMuscle SkeletalAlleleslcsh:REmbryosUbiquitinationOrganismsBiology and Life SciencesProteinsPupaeInvertebratesGenetic LociFlight AnimalMutationlcsh:QCarrier ProteinsDevelopmental Biology
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The pioneering role of PRDM9 indel mutations in tarsier evolution

2016

PRDM9 is currently the sole speciation gene found in vertebrates causing hybrid sterility probably due to incompatible alleles. Its role in defining the double strand break loci during the meiotic prophase I is crucial for proper chromosome segregation. Therefore, the rapid turnover of the loci determining zinc finger array seems to be causative for incompatibilities. We here investigated the zinc finger domain-containing exon of PRDM9 in 23 tarsiers. Tarsiers, the most basal extant haplorhine primates, exhibit two frameshifting indels at the 5'-end of the array. The first mutation event interrupts the reading frame and function while the second compensates both. The fixation of this allele…

Evolution MolecularINDEL MutationProtein DomainsTarsiidaeAnimalsZinc FingersHistone-Lysine N-MethyltransferaseArticle570 Biowissenschaften570 Life sciencesScientific Reports
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Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling

2021

Bacterial phytochrome photoreceptors usually belong to two-component signaling systems which transmit environmental stimuli to a response regulator through a histidine kinase domain. Phytochromes switch between red light-absorbing and far-red light-absorbing states. Despite exhibiting extensive structural responses during this transition, the model bacteriophytochrome from Deinococcus radiodurans (DrBphP) lacks detectable kinase activity. Here, we resolve this long-standing conundrum by comparatively analyzing the interactions and output activities of DrBphP and a bacteriophytochrome from Agrobacterium fabrum (Agp1). Whereas Agp1 acts as a conventional histidine kinase, we identify DrBphP a…

Histidine KinaseLightPROTEINSScienceAgrobacteriumHISTIDINE KINASESKinasesMolecular Dynamics SimulationPhotoreceptors MicrobialTRANSDUCTIONArticleCYANOBACTERIAL PHYTOCHROME CPH1ACTIVATIONBacterial ProteinsProtein DomainsCRYSTAL-STRUCTUREPHOSPHORYLATIONX-ray crystallographyBacterial structural biologyQREARRANGEMENTSphotoreceptorsAGROBACTERIUM-TUMEFACIENSPhosphoric Monoester HydrolasesINSIGHTSbacterial phytochromesEnzyme mechanismsbacteriaDeinococcus3111 BiomedicineSignal Transduction
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In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges

2020

Flexible spikes The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein enables viral entry into host cells by binding to the angiotensin-converting enzyme 2 (ACE2) receptor and is a major target for neutralizing antibodies. About 20 to 40 spikes decorate the surface of virions. Turoňová et al. now show that the spike is flexibly connected to the viral surface by three hinges that are well protected by glycosylation sites. The flexibility imparted by these hinges may explain how multiple spikes act in concert to engage onto the flat surface of a host cell. Science, this issue p. 203

In situElectron Microscope TomographyGlycanGlycosylationFlexibility (anatomy)virusesProtein domainPneumonia ViralHingeMolecular Dynamics SimulationBiologylaw.inventionBetacoronavirusProtein DomainslawTarget identificationmedicineHumansPandemicsResearch ArticlesHost cell surfaceMultidisciplinarySARS-CoV-2R-ArticlesCryoelectron MicroscopyBiochemCOVID-19MicrobioResearch HighlightCell biologymedicine.anatomical_structureSpike Glycoprotein Coronavirusbiology.proteinRecombinant DNASpike (software development)Protein MultimerizationStructural biologyCoronavirus InfectionsResearch ArticleScience (New York, N.y.)
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Domain shuffling between Vip3Aa and Vip3Ca: chimera stability and insecticidal activity against European, American, African, and Asian pests

2020

The bacterium Bacillus thuringiensis produces insecticidal Vip3 proteins during the vegetative growth phase with activity against several lepidopteran pests. To date, three different Vip3 protein families have been identified based on sequence identity: Vip3A, Vip3B, and Vip3C. In this study, we report the construction of chimeras by exchanging domains between Vip3Aa and Vip3Ca, two proteins with marked specificity differences against lepidopteran pests. We found that some domain combinations made proteins insoluble or prone to degradation by trypsin as most abundant insect gut protease. The soluble and trypsin-stable chimeras, along with the parental proteins Vip3Aa and Vip3Ca, were tested…

InsecticidesAsiaInsectaHealth Toxicology and Mutagenesismedicine.medical_treatmentBacillus thuringiensislcsh:MedicineSpodopteraToxicologyArticleLethal Dose 5003 medical and health sciencesHelicoverpa armigeraBacterial ProteinsProtein DomainsBacillus thuringiensismedicineAnimalsSpodoptera littoralisPest Control Biological030304 developmental biologychemistry.chemical_classification0303 health sciencesProteasebiology030306 microbiologyProtein Stabilitylcsh:RfungiSpodoptera spp.Ostrinia furnacalisSouth Americabiology.organism_classificationFusion proteinAnticarsia gemmatalisAmino acidEuropeAnticarsia gemmatalisspodoptera spp. helicoverpa armigeraBiochemistrychemistryAfricaNorth AmericaMamestra brassicaeOstrinia furnacalis
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Thermodynamics of the Interaction between the Spike Protein of Severe Acute Respiratory Syndrome Coronavirus-2 and the Receptor of Human Angiotensin-…

2020

Since the end of 2019, the coronavirus SARS-CoV-2 has caused more than 1000000 deaths all over the world and still lacks a medical treatment despite the attention of the whole scientific community. Human angiotensin-converting enzyme 2 (ACE2) was recently recognized as the transmembrane protein that serves as the point of entry of SARS-CoV-2 into cells, thus constituting the first biomolecular event leading to COVID-19 disease. Here, by means of a state-of-the-art computational approach, we propose a rational evaluation of the molecular mechanisms behind the formation of the protein complex. Moreover, the free energy of binding between ACE2 and the active receptor binding domain of the SARS…

LetterPneumonia ViralProtein domainThermodynamicsPlasma protein bindingMolecular Dynamics SimulationPeptidyl-Dipeptidase ALigandsmedicine.disease_causeProtein-Protein Binding01 natural sciencesDockingBetacoronavirus03 medical and health sciencesProtein Domains0103 physical sciencesmedicineHumansGeneral Materials SciencePhysical and Theoretical ChemistryBinding siteReceptorPandemics030304 developmental biologyCoronaviruschemistry.chemical_classification0303 health sciencesBinding Sites010304 chemical physicsSARS-CoV-2Spike ProteinCOVID-19PlicamycinTransmembrane proteinEnzymechemistrySettore CHIM/03 - Chimica Generale E InorganicaMolecular Dynamics SimulationsSpike Glycoprotein CoronavirusAngiotensin-converting enzyme 2DiosminThermodynamicsAngiotensin-Converting Enzyme 2Coronavirus InfectionsProtein Binding
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The STAT3 Inhibitor Galiellalactone Reduces IL6-Mediated AR Activity in Benign and Malignant Prostate Models

2018

IL6/STAT3 signaling is associated with endocrine therapy resistance in prostate cancer, but therapies targeting this pathway in prostate cancer were unsuccessful in clinical trials so far. The mechanistic explanation for this phenomenon is currently unclear; however, IL6 has pleiotropic effects on a number of signaling pathways, including the androgen receptor (AR). Therefore, we investigated IL6-mediated AR activation in prostate cancer cell lines and ex vivo primary prostate tissue cultures in order to gain a better understanding on how to inhibit this process for future clinical trials. IL6 significantly increased androgen-dependent AR activity in LNCaP cells but importantly did not infl…

Male0301 basic medicineCancer ResearchINTERLEUKIN-6LactonesProstate cancerLIGAND-INDEPENDENT ACTIVATION0302 clinical medicineProstateDEPRIVATIONANDROGEN RECEPTORGLUCOCORTICOID-RECEPTORmedicine.anatomical_structureOncologyReceptors Androgen030220 oncology & carcinogenesisAndrogensSILTUXIMAB CNTO 328GROWTHSIGNAL TRANSDUCERSignal transductionLife Sciences & BiomedicineProtein BindingSignal TransductionSTAT3 Transcription FactorENZALUTAMIDEmedicine.drug_classMice NudeModels BiologicalTMPRSS203 medical and health sciencesProtein DomainsCell Line TumorLNCaPmedicineAnimalsHumansCastrationCANCER CELLSScience & TechnologyInterleukin-6business.industryProstatic NeoplasmsDNAmedicine.diseaseAndrogenXenograft Model Antitumor AssaysAndrogen receptor030104 developmental biologyCancer researchbusinessEx vivo
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