Search results for "BINDING DOMAIN"

showing 10 items of 81 documents

Interaction ofEscherichia colihemolysin with biological membranes

2001

Escherichia coli hemolysin (HlyA) is a membrane-permeabilizing protein belonging to the family of RTX-toxins. Lytic activity depends on binding of Ca2(+) to the C-terminus of the molecule. The N-terminus of HlyA harbors hydrophobic sequences that are believed to constitute the membrane-inserting domain. In this study, 13 HlyA cysteine-replacement mutants were constructed and labeled with the polarity-sensitive fluorescent probe 6-bromoacetyl-2-dimethylaminonaphthalene (badan). The fluorescence emission of the label was examined in soluble and membrane-bound toxin. Binding effected a major blue shift in the emission of six residues within the N-terminal hydrophobic domain, indicating inserti…

Conformational changeProtein ConformationPlasma protein bindingBiologymedicine.disease_causeHemolysisBiochemistryHemolysin ProteinsProtein structureBacterial Proteins2-NaphthylamineEscherichia colimedicineCysteineCloning MolecularLipid bilayerEscherichia coliFluorescent DyesEscherichia coli ProteinsCell MembraneErythrocyte MembraneBiological membraneProtein Structure TertiarySpectrometry FluorescenceMembraneBiochemistryMutagenesisLiposomesChromatography GelCalciumElectrophoresis Polyacrylamide GelProtein BindingBinding domainEuropean Journal of Biochemistry
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Human Inducible Hsp70: Structures, Dynamics, and Interdomain Communication from All-Atom Molecular Dynamics Simulations

2015

The 70 kDa human heat shock protein is a major molecular chaperone involved in de novo folding of proteins in vivo and refolding of proteins under stress conditions. Hsp70 is related to several "misfolding diseases" and other major pathologies, such as cancer, and is a target for new therapies. Hsp70 is comprised of two main domains: an N-terminal nucleotide binding domain (NBD) and a C-terminal substrate protein binding domain (SBD). The chaperone function of Hsp70 is based on an allosteric mechanism. Binding of ATP in NBD decreases the affinity of the substrate for SBD, and hydrolysis of ATP is promoted by binding of polypeptide segments in the SBD. No complete structure of human Hsp70 is…

Conformational changebiologySaccharomyces cerevisiaeAllosteric regulationPlasma protein bindingbiology.organism_classificationComputer Science ApplicationsMolecular dynamicsBiochemistryCyclic nucleotide-binding domainATP hydrolysisChaperone (protein)biology.proteinBiophysicsPhysical and Theoretical ChemistryJournal of Chemical Theory and Computation
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The structural plasticity of the C terminus of p21Cip1 is a determinant for target protein recognition.

2003

The cyclin-dependent kinase inhibitory protein p21(Cip1) might play multiple roles in cell-cycle regulation through interaction of its C-terminal domain with a defined set of cellular proteins such as proliferating cell nuclear antigen (PCNA), calmodulin (CaM), and the oncoprotein SET. p21(Cip1) could be described as an intrinsically unstructured protein in solution although the C-terminal domain adopts a well-defined extended conformation when bound to PCNA. However, the molecular mechanism of the interaction with CaM and the oncoprotein SET is not well understood, partly because of the lack of structural information. In this work, a peptide derived from the C-terminal domain of p21(Cip1) …

Cyclin-Dependent Kinase Inhibitor p21Models MolecularMagnetic Resonance SpectroscopyCalmodulinChromosomal Proteins Non-HistoneProtein ConformationPeptideBiologyLigandsBiochemistryBinding CompetitiveDomain (software engineering)Molecular recognitionCalmodulinCyclinsProliferating Cell Nuclear AntigenEscherichia coliHumansHistone ChaperonesMolecular Biologychemistry.chemical_classificationC-terminusCircular DichroismOrganic ChemistryCell CycleProteinsPeptide FragmentsCell biologyDNA-Binding ProteinschemistryBiochemistrybiology.proteinMolecular MedicineTarget proteinAlpha helixBinding domainTranscription FactorsChembiochem : a European journal of chemical biology
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Sex-specific windows for high mRNA expression of DNA methyltransferases 1 and 3A and methyl-CpG-binding domain proteins 2 and 4 in human fetal gonads

2006

DNA methyltransferases (DNMTs) and 5-methyl-CpG-binding domain proteins (MBDs) are involved in the acquisition of parent-specific epigenetic modifications in human male and female germ cells. Reverse Northern blot analyses demonstrated sex-specific differences in mRNA expression for the maintenance DNMT1 and the de novo DNMT3A in developing testis and ovary. In fetal testis DNMT1 and DNMT3A expression peaked in mitotically arrested spermatogonia around 21 weeks gestation. In fetal ovary transcriptional upregulation of DNMT1 and DNMT3A occurred during a very brief period at 16 weeks gestation, when the oocytes proceeded through meiotic prophase. Fetal gonads showed several fold higher DNMT3A…

DNA (Cytosine-5-)-Methyltransferase 1MaleMethyltransferaseEmbryonic DevelopmentGestational AgeOvaryBiologyGene Expression Regulation EnzymologicChromatin remodelingDNA Methyltransferase 3AFetal DevelopmentPregnancyTestisGeneticsmedicineHumansDNA (Cytosine-5-)-MethyltransferasesRNA MessengerEpigeneticsRegulation of gene expressionFetusReverse Transcriptase Polymerase Chain Reactionurogenital systemOvaryGene Expression Regulation DevelopmentalCell BiologyReverse northern blotMolecular biologyMethyl-CpG-binding domainCell biologyDNA-Binding Proteinsmedicine.anatomical_structureembryonic structuresFemaleTranscription FactorsDevelopmental BiologyMolecular Reproduction and Development
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Molecular cloning and expression of Tenebrio molitor ultraspiracle during metamorphosis and in vivo induction of its phosphorylation by 20-hydroxyecd…

2000

Using a RT-PCR approach, the Tenebrio molitor homologue of Drosophila Ultraspiracle (TmUSP) was characterized. Its DNA binding domain shows a degree of identity with those of the other insect USPs. However, the ligand binding domain is closer to those of retinoid X receptors. Using an antibody raised against DmUSP, Western blot analysis of proteins from epidermis and other tissues revealed five immunoreactive bands, corresponding to different phosphorylated forms of a unique polypeptide, as shown by lambda-phosphatase treatment. The nuclear form of TmUSP seems unphosphorylated. An in vivo 20-hydroxyecdysone treatment increases considerably and rapidly the phosphorylated forms of TmUSP. This…

DNA ComplementaryMolecular Sequence Data20-HydroxyecdysoneGene ExpressionMolecular cloningBiologychemistry.chemical_compoundWestern blotGene expressionGeneticsmedicineAnimalsDrosophila ProteinsHumansProtein IsoformsAmino Acid SequenceRNA MessengerCloning MolecularPhosphorylationReceptorTenebrioMolecular BiologyEpidermis (botany)medicine.diagnostic_testMetamorphosis BiologicalDNA-binding domainSequence Analysis DNAMolecular biologyCell biologyDNA-Binding ProteinsEcdysteronechemistryInsect SciencePhosphorylationEpidermisTranscription FactorsInsect molecular biology
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Isolation and characterization of five Fox (Forkhead) genes from the sponge Suberites domuncula.

2003

Fox or Forkhead genes constitute a subgroup of the helix-turn-helix class of transcription factors with a characteristic and highly conserved DNA binding domain. To date, around 100 different Fox genes have been reported ranging from yeast to humans; these have been classified into 18 subclasses (A to P). Fox proteins are responsible for a wide range of functions and key roles in early developmental processes, during organogenesis and also for the function of the major organs and tissues in the adult. Here, we report the isolation and phylogenetic characterization of five members of the Fox family from the sponge Suberites domuncula. Four of them (Sd-FoxL2, Sd-FoxP, Sd-FoxD and Sd-FoxF) fal…

DNA ComplementaryTime FactorsSequence analysisMolecular Sequence DataSequence alignmentBiologyFOX proteinsPhylogeneticsparasitic diseasesGeneticsAnimalsCloning MolecularGeneCells CulturedPhylogenyGeneticsSequence Homology Amino AcidGene Expression ProfilingGeneral MedicineDNA-binding domainAnatomySequence Analysis DNAbiology.organism_classificationPoriferaSuberites domunculaSpongeMultigene FamilySequence AlignmentTranscription FactorsGene
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A peptide inhibiting the collagen binding function of integrin alpha2I domain.

1999

Integrin alpha2 subunit forms in the complex with the beta1 subunit a cell surface receptor binding extracellular matrix molecules, such as collagens and laminin-1. It is a receptor for echovirus-1, as well. Ligands are recognized by the special "inserted" domain (I domain) in the integrin alpha2 subunit. Venom from a pit viper, Bothrops jararaca, has been shown to inhibit the interaction of platelet alpha2beta1 integrin with collagen because of the action of a disintegrin/metalloproteinase named jararhagin. The finding that crude B. jararaca venom could prevent the binding of human recombinant ralpha2I domain to type I collagen led us to study jararhagin further. Synthetic peptides represe…

EGF-like domainIntegrinIntegrin alpha2PeptideBiologyBiochemistryPeptides CyclicEuropiumAntigens CDCrotalid VenomsDisintegrinHumansAmino Acid SequenceMolecular BiologyRGD motifDNA Primerschemistry.chemical_classificationBase SequenceCell MembraneMetalloendopeptidasesCell BiologyCyclic peptideRecombinant ProteinsBiochemistrychemistryJararhaginbiology.proteinCollagenBinding domainThe Journal of biological chemistry
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Crystal structure of human gamma-butyrobetaine hydroxylase.

2010

Gamma-butyrobetaine hydroxylase (GBBH) is a 2-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of l-carnitine by hydroxylation of gamma-butyrobetaine (GBB). l-carnitine is required for the transport of long-chain fatty acids into mitochondria for generating metabolic energy. The only known synthetic inhibitor of GBBH is mildronate (3-(2,2,2-trimethylhydrazinium) propionate dihydrate), which is a non-hydroxylatable analog of GBB. To aid in the discovery of novel GBBH inhibitors by rational drug design, we have solved the three-dimensional structure of recombinant human GBBH at 2.0A resolution. The GBBH monomer consists of a catalytic double-stranded beta-helix (DBSH) domai…

EGF-like domainStereochemistrygamma-Butyrobetaine DioxygenaseBiophysicsDrug designBiochemistryHydroxylationchemistry.chemical_compoundDioxygenaseCatalytic DomainHumansEnzyme InhibitorsMolecular BiologyHistidinechemistry.chemical_classificationCrystallographybiologyActive siteCell BiologyRecombinant ProteinsZincEnzymeBiochemistrychemistryCyclic nucleotide-binding domainDrug Designbiology.proteinProtein MultimerizationMethylhydrazinesBiochemical and biophysical research communications
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Methyl-CpG-binding domain sequencing reveals a prognostic methylation signature in neuroblastoma

2016

Accurate assessment of neuroblastoma outcome prediction remains challenging. Therefore, this study aims at establishing novel prognostic tumor DNA methylation biomarkers. In total, 396 low- and high-risk primary tumors were analyzed, of which 87 were profiled using methyl-CpG-binding domain (MBD) sequencing for differential methylation analysis between prognostic patient groups. Subsequently, methylation-specific PCR (MSP) assays were developed for 78 top-ranking differentially methylated regions and tested on two independent cohorts of 132 and 177 samples, respectively. Further, a new statistical framework was used to identify a robust set of MSP assays of which the methylation score (i.e.…

EXPRESSIONMale0301 basic medicineGENESPROMOTERBIOMARKERSMedizinComputational biologyBiologyPHENOTYPEReal-Time Polymerase Chain ReactionCohort StudiesneuroblastomaNeuroblastoma03 medical and health sciencesPOOR-PROGNOSISSTRATIFICATIONNeuroblastomaMedicine and Health SciencesTumor Cells CulturedmedicineHumansNeoplasm StagingGeneticsDNA methylationBinding SitesComputational BiologyInfantDNADNA NeoplasmMethylationPrognosismedicine.diseaseMethyl-CpG-binding domain030104 developmental biologyDifferentially methylated regionsReal-time polymerase chain reactionRISK GROUPOncologyCpG siteSTAGE-4 NEUROBLASTOMADNA methylationbiomarkerBiomarker (medicine)CpG IslandsFemaleprognosisBiomarkersResearch PaperOncotarget
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Functional analysis of the isoforms of an ABI3-like factor of Pisum sativum generated by alternative splicing

2009

At least seven isoforms (PsABI3-1 to PsABI3-7) of a putative, pea ABI3-like factor, originated by alternative splicing, have been identified after cDNA cloning. A similar variability had previously only been described for monocot genes. The full-length isoform, PsABI3-1, contains the typical N-terminal acidic domains and C-terminal basic subdomains, B1 to B3. Reverse transcriptase-PCR analysis revealed that the gene is expressed just in seeds, starting at middle embryogenesis; no gene products are observed in embryo axes after 18 h post-imbibition although they are more persistent in cotyledons. The activity of the isoforms was studied by yeast one-hybrid assays. When yeast was transformed …

Gene isoformABI3PhysiologyABI5Molecular Sequence DataPlant ScienceBiologyAbscisic acidComplementary DNAGene expressionProtein IsoformsArabidopsis thalianaAmino Acid SequenceCloning MolecularGenePlant ProteinsBase SequenceAlternative splicingisoformsPeasfood and beveragesDNA-binding domainbiology.organism_classificationResearch PapersAlternative SplicingProtein TransportABABiochemistryRNA splicingProtein BindingJournal of Experimental Botany
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