Search results for "lysine"

showing 10 items of 170 documents

Structural Characterization of Set1 RNA Recognition Motifs and their Role in Histone H3 Lysine 4 Methylation

2006

Departament de Bioquimica iBiologia Molecular, Universitatde Valencia, C/Dr Moliner 50,46100, Burjassot, SpainThe yeast Set1 histone H3 lysine 4 (H3K4) methyltransferase contains, inaddition to its catalytic SET domain, a conserved RNA recognition motif(RRM1). We present here the crystal structure and the secondary structureassignment in solution of the Set1 RRM1. Although RRM1 has the expectedβαββαβ RRM-fold, it lacks the typical RNA-binding features of thesemodules. RRM1 is not able to bind RNA by itself in vitro, but a constructcombining RRM1 with a newly identified downstream RRM2 specificallybinds RNA. Invivo,H3K4 methylation isnot affectedbyapoint mutation inRRM2 that preserves Set1 s…

Models MolecularRiboswitchHistone H3 Lysine 4Saccharomyces cerevisiae ProteinsRNA-induced transcriptional silencingSurface Properties[SDV]Life Sciences [q-bio]Molecular Sequence DataSaccharomyces cerevisiae[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]BiologyMethylationHistonesStructure-Activity Relationship03 medical and health sciencesStructural BiologyHistone methylation[SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Amino Acid SequenceProtein Structure QuaternaryMolecular BiologyConserved Sequence030304 developmental biology0303 health sciencesRNA recognition motifLysine030302 biochemistry & molecular biologyRNARNA FungalHistone-Lysine N-MethyltransferaseNon-coding RNAMolecular biology[SDV] Life Sciences [q-bio]DNA-Binding ProteinsProtein SubunitsBiochemistryHistone methyltransferaseSequence AlignmentProtein BindingTranscription Factors
researchProduct

Factors Dictating the Pseudocatalytic Efficiency of Avidins

2006

The hydrolysis of biotinyl p-nitrophenyl ester (BNP) by a series of avidin derivatives was examined. Surprisingly, a hyperthermostable avidin-related protein (AVR4) was shown to display extraordinary yet puzzling hydrolytic activity. In order to evaluate the molecular determinants that contribute to the reaction, the crystal structure of AVR4 was compared with those of avidin, streptavidin and key mutants of the two proteins in complex with biotinyl p-nitroanilide (BNA), the inert amide analogue of BNP. The structures revealed that a critical lysine residue contributes to the hydrolysis of BNP by avidin but has only a minor contribution to the AVR4-mediated reaction. Indeed, the respective …

Models MolecularStreptavidinNitrogenStereochemistryLysineGene ExpressionPlasma protein bindingCrystallography X-RayCatalysischemistry.chemical_compoundProtein structureNucleophileStructural BiologyAmideMolecular BiologyBinding SitesbiologyChemistryHydrolysisLysinePhenyl EthersAvidinLigand (biochemistry)Recombinant ProteinsProtein Structure TertiaryStructural Homology ProteinMutationbiology.proteinStreptavidinProtein BindingAvidinJournal of Molecular Biology
researchProduct

Calculation of binding energy using BLYP/MM for the HIV-1 integrase complexed with the S-1360 and two analogues.

2007

Abstract Integrase (IN) is one of the three human immunodeficiency virus type 1 (HIV-1) enzymes essential for effective viral replication. S-1360 is a potent and selective inhibitor of HIV-1 IN. In this work, we have carried out molecular dynamics (MD) simulations using a hybrid Quantum Mechanics/Molecular Mechanics (QM/MM) approach, to determine the protein–ligand interaction energy for S-1360 and two analogues. Analysis of the MD trajectories reveals that the strongest protein–inhibitor interactions, observed in the three studied complexes, are established with Lys-159 residue and Mg 2+ cation. Calculations of binding energy using BLYP/MM level of theory reveal that there is a direct rela…

Molecular modelStereochemistryProtein ConformationClinical BiochemistryBinding energyPharmaceutical ScienceHIV IntegraseCrystallography X-RayBiochemistryMolecular mechanicsMolecular dynamicsPropaneStructure-Activity RelationshipDrug DiscoveryHumansMagnesiumPyrrolesAmino Acid SequenceHIV Integrase InhibitorsFuransMolecular Biologychemistry.chemical_classificationbiologyChemistryLysineOrganic ChemistryActive siteInteraction energyTriazolesIntegraseEnzymeAmino Acid SubstitutionModels Chemicalbiology.proteinMolecular MedicineBioorganicmedicinal chemistry
researchProduct

FSHD muscular dystrophy region gene 1 binds Suv4-20h1 histone methyltransferase and impairs myogenesis.

2013

Facioscapulohumeral muscular dystrophy (FSHD) is an autosomal dominant myopathy with a strong epigenetic component. It is associated with deletion of a macrosatellite repeat leading to over-expression of the nearby genes. Among them, we focused on FSHD region gene 1 (FRG1) since its over-expression in mice, Xenopus laevis and Caenorhabditis elegans, leads to muscular dystrophy-like defects, suggesting that FRG1 plays a relevant role in muscle biology. Here we show that, when over-expressed, FRG1 binds and interferes with the activity of the histone methyltransferase Suv4-20h1 both in mammals and Drosophila. Accordingly, FRG1 over-expression or Suv4-20h1 knockdown inhibits myogenesis. Moreov…

Muscle DevelopmentEvolution Molecular03 medical and health sciencesMice0302 clinical medicineGeneticsmedicineFacioscapulohumeral muscular dystrophyMyocyteAnimalsHumansEpigeneticsMuscular dystrophyMyopathyMolecular Biology030304 developmental biologyCell NucleusMice Knockout0303 health sciencesMuscle CellsbiologyMyogenesisMicrofilament ProteinsNuclear ProteinsProteinsRNA-Binding ProteinsCell DifferentiationCell BiologyGeneral MedicineHistone-Lysine N-MethyltransferaseMuscular Dystrophy Animalmedicine.diseaseMolecular biologyHistoneDrosophila melanogasterHEK293 CellsPhenotypeOrgan SpecificityHistone methyltransferaseEpigenetic deregulation by FRG1Gene Knockdown Techniquesbiology.proteinmedicine.symptomCarrier Proteins030217 neurology & neurosurgeryProtein BindingJournal of molecular cell biology
researchProduct

The Candida albicans pH-regulated KER1 gene encodes a lysine/glutamic-acid-rich plasma-membrane protein that is involved in cell aggregation.

2004

Immunoscreening of aCandida albicanscDNA library with a polyclonal germ-tube-specific antibody (pAb anti-gt) resulted in the isolation of a gene encoding a lysine/glutamic-acid-rich protein, which was consequently designatedKER1. The nucleotide and deduced amino acid sequences of this gene displayed no significant homology with any other known sequence.KER1encodes a 134 kDa lysine (14·5 %)/glutamic acid (16·7 %) protein (Ker1p) that contains two potential transmembrane segments.KER1was expressed in a pH-conditional manner, with maximal expression at alkaline pH and lower expression at pH 4·0, and was regulated byRIM101. A Δker1/Δker1null mutant grew normally but was hyperflocculant under ge…

MutantLysineGenes FungalMolecular Sequence DataGlutamic AcidMicrobiologyFungal ProteinsMiceImmunoscreeningComplementary DNAGene Expression Regulation FungalCandida albicansAnimalsCloning MolecularCandida albicansDNA Fungalchemistry.chemical_classificationbiologyBase SequenceVirulenceLysineMembrane ProteinsHydrogen-Ion Concentrationbiology.organism_classificationMolecular biologyTransmembrane proteinAmino acidPhenotypechemistryBiochemistryPolyclonal antibodiesMice Inbred DBAbiology.proteinGene DeletionSubcellular FractionsMicrobiology (Reading, England)
researchProduct

CCDC 1874606: Experimental Crystal Structure Determination

2019

Related Article: Olga Schäfer, Dieter Schollmeyer, Alexander Birke, Regina Holm, Kerstin Johann, Christian Muhl, Christine Seidl, Benjamin Weber, Matthias Barz|2019|Tetrahedron Lett.|60|272|doi:10.1016/j.tetlet.2018.12.028

N-epsilon-t-butyloxycarbonyl-L-lysine N-carboxyanhydrideSpace GroupCrystallographyCrystal SystemCrystal StructureCell ParametersExperimental 3D Coordinates
researchProduct

Synergistic targeting of FLT3 mutations in AML via combined menin-MLL and FLT3 inhibition

2020

Abstract The interaction of menin (MEN1) and MLL (MLL1, KMT2A) is a dependency and provides a potential opportunity for treatment of NPM1-mutant (NPM1mut) and MLL-rearranged (MLL-r) leukemias. Concomitant activating driver mutations in the gene encoding the tyrosine kinase FLT3 occur in both leukemias and are particularly common in the NPM1mut subtype. In this study, transcriptional profiling after pharmacological inhibition of the menin-MLL complex revealed specific changes in gene expression, with downregulation of the MEIS1 transcription factor and its transcriptional target gene FLT3 being the most pronounced. Combining menin-MLL inhibition with specific small-molecule kinase inhibitors…

NPM1Transcription GeneticImmunologyApoptosisBiochemistryMiceRandom AllocationMice Inbred NODCell Line TumorProto-Oncogene Proteinshemic and lymphatic diseasesAntineoplastic Combined Chemotherapy ProtocolsGene expressionmedicineAnimalsHumansMEN1PhosphorylationMyeloid Ecotropic Viral Integration Site 1 ProteinProtein Kinase InhibitorsneoplasmsbiologyGene Expression Regulation LeukemicKinaseNuclear ProteinsMyeloid leukemiaDrug SynergismHistone-Lysine N-MethyltransferaseCell BiologyHematologymedicine.diseaseCoculture TechniquesNeoplasm ProteinsLeukemia Myeloid AcuteLeukemiaKMT2Afms-Like Tyrosine Kinase 3biology.proteinCancer researchNucleophosminProtein Processing Post-TranslationalTyrosine kinaseMyeloid-Lymphoid Leukemia ProteinBlood
researchProduct

Single cigar-shaped nanopores functionalized with amphoteric amino acid chains: experimental and theoretical characterization.

2012

We present an experimental and theoretical characterization of single cigar-shaped nanopores with pH-responsive carboxylic acid and lysine chains functionalized on the pore surface. The nanopore characterization includes (i) optical images of the nanostructure obtained by FESEM; (ii) different chemical procedures for the nanopore preparation (etching time and functionalizations; pH and electrolyte concentration of the external solution) allowing externally tunable nanopore responses monitored by the current-voltage (I-V) curves; and (iii) transport simulations obtained with a multilayer nanopore model. We show that a single, approximately symmetric nanopore can be operated as a reconfigurab…

NanoporeRe-configurablePHAmino acid chainsEtching timeElectrical signalCarboxylic AcidsGeneral Physics and AstronomyFunctionalizationsElectrolytePore surfaceElectrochemistryFunctionalizedCarboxylic acidOptical imageNanoporesElectric conductivityI - V curveElectrochemistryGeneral Materials ScienceTheoretical modelRectifying behaviorsFundamental conceptsRectifying propertiesSurface propertyGeneral EngineeringHydrogen-Ion ConcentrationCigar-shaped nanoporeCharacterization (materials science)Data processingChemistryNanoporeAmino acidsIon channelTransport simulationIodineLogic functionsNanostructureMaterials scienceLogicSurface PropertiesCharacterizationNanotechnologyTunabilitiesArticleDrug controlled releaseElectrical resistivity and conductivityEtchingTransport processPH-responsiveCurrent voltage curveDiodeChemical proceduresCarboxylic acidsLysineElectric ConductivityModels TheoreticalGeometrical opticsNanostructuresAmphoteric amino acid chainsCurrent-voltage curvesExternal solutionsFISICA APLICADAElectrolyte concentrationACS nano
researchProduct

Solid-state NMR investigation on the interactions between a synthetic montmorillonite and two homopolypeptides.

2006

Abstract Interactions of two homopolypeptides (polylysine and polyglutamic acid) with a synthetic montmorillonite were studied by 1H MAS, 1H–27Al HETCOR and 1H–13C CP-MAS NMR experiments. 1H–27Al HETCOR with 1H spin-diffusion NMR appears to be a powerful probe for the identification of the polypeptide fragments, which interact with the montmorillonite interlayer surfaces. In particular, selective interactions were observed between the polypeptide side-chains and the montmorillonite octahedral aluminum atoms. 1H–13C CP-MAS NMR experiments were used to assess the dynamics of the two polypeptides through the measurement of the t1/2 characteristic time of selected carbons. Results indicate that…

Nuclear and High Energy PhysicsRadiationMagnetic Resonance SpectroscopyPolyglutamic acidGeneral Chemistrychemistry.chemical_compoundKineticsSoilAdsorptionMontmorilloniteOctahedronchemistrySolid-state nuclear magnetic resonancePolylysinePolymer chemistrySide chainBentonitePeptidesInstrumentationSolid state nuclear magnetic resonance
researchProduct

Evolution of available lysine and furosine contents in milk-based infant formulas throughout the shelf-life storage period

2003

The evolution of the Maillard reaction (MR) by measuring the available lysine and furosine (FUR) contents in adapted and follow-up powdered milk-based infant formulas over the shelf-life storage period, at 20 and 37 °C, was studied. Available lysine and FUR contents were determined by fluorimetry and high-performance liquid chromatography respectively. Statistically significant differences were found between adapted and follow-up infant formulas with respect to the available lysine and FUR contents. Available lysine contents decreased significantly throughout the storage time, and the contents at 37 °C were lower than at 20 °C. A statistically significant increase in FUR contents was observ…

Nutrition and DieteticsChemistryLysineFood preservationShelf lifecomplex mixturesMaillard reactionsymbols.namesakeInfant formulasymbolsbacteriaFood scienceAgronomy and Crop ScienceFood ScienceBiotechnologyJournal of the Science of Food and Agriculture
researchProduct