Search results for "binding site"

showing 10 items of 856 documents

Functional characterization of Tat protein from human immunodeficiency virus. Evidence that Tat links viral RNAs to nuclear matrix.

1990

The processes of transcription and posttranscription are assumed to proceed in close association with the nuclear matrix. In this study we demonstrated that Tat, the trans-activating protein from human immunodeficiency virus type 1 (HIV-1), binds both to the TAR region of the nascent HIV mRNAs and the nuclear matrix with high affinity. Both North/Western blotting experiments and nitrocellulose binding studies revealed that Tat binds with an association constant (K alpha) of approximately 1 x 10(9) M-1 to the TAR segment of HIV RNA; binding of Tat to this sequence which is present between position 32 and 82 downstream from the TATA box was also confirmed by gel retardation assays. Binding of…

Messenger RNAViral matrix proteinTranscription GeneticTATA boxBinding proteinGene Products gagCell BiologyBiologyNuclear matrixBiochemistryMolecular biologyCell LineTranscription (biology)Gene Products tatHIV-1Trans-ActivatorsHumansRNA ViralNuclear Matrixtat Gene Products Human Immunodeficiency VirusCloning MolecularBinding siteMolecular BiologyProtein secondary structure
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DeepSRE: Identification of sterol responsive elements and nuclear transcription factors Y proximity in human DNA by Convolutional Neural Network anal…

2021

SREBP1 and 2, are cholesterol sensors able to modulate cholesterol-related gene expression responses. SREBPs binding sites are characterized by the presence of multiple target sequences as SRE, NFY and SP1, that can be arranged differently in different genes, so that it is not easy to identify the binding site on the basis of direct DNA sequence analysis. This paper presents a complete workflow based on a one-dimensional Convolutional Neural Network (CNN) model able to detect putative SREBPs binding sites irrespective of target elements arrangements. The strategy is based on the recognition of SRE linked (less than 250 bp) to NFY sequences according to chromosomal localization derived from …

Metabolic ProcessesSettore MED/09 - Medicina InternaConservation BiologyGene ExpressionBiochemistryConservation ScienceData ManagementRegulation of gene expressionMultidisciplinaryGene OntologiesQRGenomicsLipidsPhylogeneticsCholesterolConservation GeneticsMedicineSettore MED/46 - Scienze Tecniche Di Medicina Di LaboratorioResearch ArticleComputer and Information SciencesSp1 Transcription FactorSequence analysisScienceDNA transcriptionComputational biologyBiologyData mining Deep Learning Genetics Transcription factorDNA-binding proteinsGeneticsHumansGene RegulationEvolutionary SystematicsBinding siteGeneTranscription factorTaxonomyEvolutionary BiologyModels GeneticEcology and Environmental SciencesBiology and Life SciencesComputational BiologyProteinsPromoterDNA PatternsDNASequence Analysis DNAGenome AnalysisRegulatory ProteinsSterol regulatory element-binding proteinMetabolismSerum Response ElementCCAAT-Binding FactorTranscription Factors
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Poly-Xaa Sequences in Proteins - Biological Role and Interactions with Metal Ions: Chemical and Medical Aspects

2016

Background: The understanding of the bioinorganic and coordination chemistry of metalloproteins containing unusual poly-Xaa sequences, in which a single amino acid is repeated consecutively, is crucial for describing their metal binding-structure-function relationship, and therefore also crucial for understanding their medicinal potential. To the best of our knowledge, this is the first systematic review on metal complexes with polyXaa sequences. Methods: We performed a thorough search of high quality peer reviewed literature on poly-Xaa type of sequences in proteins, focusing on their biological importance and on their interactions with metal ions. Results: 228 papers were included in the…

Metal ions in aqueous solutionComputational biology010402 general chemistry01 natural sciencesBiochemistryCoordination complexTurn (biochemistry)metal chaperonesCoordination ComplexesDrug DiscoveryMetalloproteinHumansAmino Acid SequenceSingle amino acidAmino AcidsBinding siteantimicrobial therapeuticsIonsPharmacologychemistry.chemical_classification010405 organic chemistryMetal bindingOrganic Chemistrymetal ionsProteinsBioinorganic chemistry0104 chemical scienceschemistryChemical physicsMetal-protein complexespoly-Xaa peptide sequencesMolecular MedicineCurrent Medicinal Chemistry
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Cobalt(IV) corroles as catalysts for the electroreduction of O2: reactions of heterobimetallic dyads containing a face-to-face linked Fe(III) or Mn(I…

2006

Abstract A series of heterobinuclear cofacial porphyrin–corrole dyads containing a Co(IV) corrole linked by one of four different spacers in a face-to-face arrangement with an Fe(III) or Mn(III) porphyrin have been examined as catalysts for the electroreduction of O 2 to H 2 O and/or H 2 O 2 when adsorbed on the surface of a graphite electrode in air-saturated aqueous solutions containing 1 M HClO 4 . The examined compounds are represented as (PCY)M III ClCo IV Cl where P is a porphyrin dianion, C is a corrole trianion and Y is a biphenylene (B), 9,9-dimethylxanthene (X), dibenzofuran (O) or anthracene (A) spacer. The catalytic behavior of the seven investigated dyads in the two heterobimet…

Metalloporphyrinschemistry.chemical_element010402 general chemistryElectrochemistryElectrocatalystPhotochemistryporphyrins01 natural sciencesBiochemistryMedicinal chemistryFerric CompoundsCatalysisCatalysisInorganic Chemistrychemistry.chemical_compoundElectron transfer[ CHIM.CATA ] Chemical Sciences/Catalysiscatalytic dioxygen reductionCorrolecorrolesComputingMilieux_MISCELLANEOUSManganeseBinding Sites010405 organic chemistryCobalt[CHIM.CATA]Chemical Sciences/CatalysisBiphenylenePorphyrin0104 chemical sciencesOxygenchemistryelectrochemistryCobaltOxidation-Reduction
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The Independent Biological Activity of Bacillus thuringiensis Cry23Aa Protein Against Cylas puncticollis

2020

The Cry23Aa/Cry37Aa proteins from Bacillus thuringiensis (Bt) have been described toxic to Cylas puncticollis larvae. In general, it is believed that Cry23Aa and Cry37Aa act jointly to exert the insecticidal activity, while there is no evidence of their toxicity individually. Therefore, in the present study, the contribution of each protein in the insecticidal activity toward C. puncticollis larvae has been assessed. The results showed that both proteins were toxic for C. puncticollis larvae when tested individually. Contrary to what was claimed previously, our results suggest that the presence of both proteins is not necessary to exert toxicity against C. puncticollis larvae. Also, the bin…

Microbiology (medical)Agriculture and Food SciencesSWEET-POTATO WEEVILlcsh:QR1-502sweet potato weevilsbinary toxinMicrobiologylcsh:Microbiology03 medical and health sciencesmode of actioninsecticidal proteinsBacillus thuringiensisBioassayCry37AaBinding siteSPHAERICUS TOXINMode of action030304 developmental biologybinding assay0303 health sciencesPore-forming toxinLarvabiology030306 microbiologyCRYSTAL PROTEINCOMPONENTSfungiMidgutBiological activityBORDER MEMBRANE-VESICLESENTOMOPATHOGENIC FUNGIbiology.organism_classificationEFFICACYBiochemistrybioassayCOLEOPTERABRUNNEUSRESISTANCEFrontiers in Microbiology
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Sensing by the membrane-bound sensor kinase DcuS: exogenous versus endogenous sensing of C(4)-dicarboxylates in bacteria.

2010

Bacteria are able to grow at the expense of both common (succinate, L-malate, fumarate and aspartate) and uncommon (L-tartrate and D-malate) C4-dicarboxylates, which are components of central metabolism. Two types of sensors/regulators responding to the C4-dicarboxylates function in Escherichia coli, Bacillus, Lactobacillus and related bacteria. The first type represents membrane-integral two-component systems, while the second includes cytoplasmic LysR-type transcriptional regulators. The difference in location and substrate specificity allows the exogenous induction of metabolic genes by common C4-dicarboxylates, and endogenous induction by uncommon C4-dicarboxylates. The two-component s…

Microbiology (medical)Dicarboxylic Acid TransportersModels MolecularBacteriaEscherichia coli ProteinsCell MembraneRegulatory siteGene Expression Regulation BacterialBiologyLigand (biochemistry)MicrobiologyTransmembrane domainBiochemistryProtein kinase domainBacterial ProteinsPAS domainExtracellularEscherichia coliDicarboxylic AcidsBinding siteSignal transductionProtein KinasesSignal TransductionFuture microbiology
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Characterization of two Lactococcus lactis zinc membrane proteins, Llmg_0524 and Llmg_0526, and role of Llmg_0524 in cell wall integrity

2015

Background Due to its extraordinary chemical properties, the cysteine amino acid residue is often involved in protein folding, electron driving, sensing stress, and binding metals such as iron or zinc. Lactococcus lactis, a Gram-positive bacterium, houses around one hundred cysteine-rich proteins (with the CX2C motif) in the cytoplasm, but only a few in the membrane. Results In order to understand the role played by this motif we focused our work on two membrane proteins of unknown function: Llmg_0524 and Llmg_0526. Each of these proteins has two CX2C motifs separated by ten amino-acid residues (CX2CX10CX2C). Together with a short intervening gene (llmg_0525), the genes of these two protein…

Microbiology (medical)Lysozymechemistry.chemical_elementZincPlasma protein bindingGrowthMicrobiologyMembrane proteins;Growth;Cumene hydroperoxideProtein structureBacterial ProteinsCumene hydroperoxideCell Wallcystéinelactococcus lactisMembrane proteinsBenzene Derivatives[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyCysteineBinding siteBinding SitesbiologyProtein StabilityLactococcus lactispropriété de membranebiology.organism_classificationcroissanceProtein Structure Tertiary3. Good healthZincchemistryBiochemistryMembrane proteinProtein foldingProtein BindingResearch ArticleCysteine
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Major histocompatibility complex class II binding site for streptococcal pyrogenic (erythrogenic) toxin A.

1994

Streptococcal pyrogenic exotoxin A (SPEA) is an important pathogenicity factor of group A streptococci. It is a member of the family of „superantigens” produced by Staphylococcus aureus and Streptococcus pyogenes and its T lymphocyte stimulating activity is involved into the pathogenesis of certain diseases caused by pyogenic streptococci. In this study we have produced and characterized recombinant SPEA molecules in Escherichia coli. These molecules are indistinguishable from natural SPEA in both T cell stimulatory and HLA class II binding activities. Human class II molecules are more efficient than mouse class II molecules in presenting SPEA to T cells. In binding tests to major histocomp…

Microbiology (medical)Recombinant Fusion ProteinsT-LymphocytesImmunologyAntigen presentationErythrogenic toxinBacterial ToxinsMolecular Sequence DataExotoxinsEnterotoxinmedicine.disease_causeMajor histocompatibility complexLymphocyte ActivationMicrobiologyCell LineMajor Histocompatibility ComplexEnterotoxinsMicestomatognathic systemBacterial ProteinsmedicineEscherichia coliImmunology and AllergyAnimalsHumansCells CulturedMice Inbred BALB CBinding SitesSuperantigensbiologyBase SequencePyrogensToxic shock syndromeMembrane ProteinsStreptococcusGeneral MedicineGene Expression Regulation BacterialHLA-DR Antigensmedicine.diseasebiology.organism_classificationSpeaStreptococcus pyogenesbiology.proteinExotoxinMedical microbiology and immunology
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A lipid transfer protein binds to a receptor involved in the control of plant defence responses

2001

AbstractLipid transfer proteins (LTPs) and elicitins are both able to load and transfer lipidic molecules and share some structural and functional properties. While elicitins are known as elicitors of plant defence mechanisms, the biological function of LTP is still an enigma. We show that a wheat LTP1 binds with high affinity sites. Binding and in vivo competition experiments point out that these binding sites are common to LTP1 and elicitins and confirm that they are the biological receptors of elicitins. A mathematical analysis suggests that these receptors could be represented by an allosteric model corresponding to an oligomeric structure with four identical subunits.

Models Molecular0106 biological sciencesTime FactorsProtein ConformationPlasma protein bindingLigands01 natural sciencesBiochemistryProtein structureStructural BiologyReceptorAllosteryTriticumComputingMilieux_MISCELLANEOUSPlant Proteins0303 health sciencesFungal proteinfood and beveragesCell biologyBiochemistryPlant lipid transfer proteinsAllosteric SiteProtein BindingReceptorPhytophthoraLipid transfer proteinAllosteric regulationBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyBinding CompetitiveFungal Proteins03 medical and health sciencesTobaccoGeneticsBinding site[SDV.BC] Life Sciences [q-bio]/Cellular BiologyMolecular Biology030304 developmental biologyBinding SitesDose-Response Relationship DrugAlgal ProteinsCell MembraneElicitinCell BiologyAntigens PlantModels TheoreticalLipid MetabolismElicitinCarrier Proteins010606 plant biology & botanyFEBS Letters
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In Silico Insights into the SARS CoV-2 Main Protease Suggest NADH Endogenous Defences in the Control of the Pandemic Coronavirus Infection

2020

COVID-19 is a pandemic health emergency faced by the entire world. The clinical treatment of the severe acute respiratory syndrome (SARS) CoV-2 is currently based on the experimental administration of HIV antiviral drugs, such as lopinavir, ritonavir, and remdesivir (a nucleotide analogue used for Ebola infection). This work proposes a repurposing process using a database containing approximately 8000 known drugs in synergy structure- and ligand-based studies by means of the molecular docking and descriptor-based protocol. The proposed in silico findings identified new potential SARS CoV-2 main protease (MPRO) inhibitors that fit in the catalytic binding site of SARS CoV-2 MPRO. Several sel…

Models Molecular0301 basic medicineAgingmedicine.medical_treatmentcoronaviruslcsh:QR1-502Viral Nonstructural Proteinsmedicine.disease_causelcsh:Microbiology0302 clinical medicineSettore BIO/10 - BiochimicaCoronavirus 3C ProteasesCoronavirusvirus diseasesLopinavirHypothesisMolecular Docking SimulationCysteine EndopeptidasesDrug repositioningInfectious Diseases030220 oncology & carcinogenesisCoronavirus InfectionsOxidation-Reductionmedicine.drugDNA damageIn silicoPneumonia ViralBiologyAntiviral AgentsHIV-proteaseBetacoronavirus03 medical and health sciencesSARS-CoV-2 main proteaseVirologymedicineHumansComputer SimulationProtease InhibitorsPandemicsBinding SitesProteaseSARS-CoV-2Drug RepositioningCOVID-19HIV Protease InhibitorsDRUDIT web servicemolecular dockingNADbiology.organism_classificationVirologySettore CHIM/08 - Chimica FarmaceuticaCOVID-19 Drug Treatmentcoronaviru030104 developmental biologyNADHRitonavirBetacoronavirusDNA Damage
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