Search results for "binding site"

showing 10 items of 856 documents

RNA nucleotide methylation

2011

Methylation of RNA occurs at a variety of atoms, nucleotides, sequences and tertiary structures. Strongly related to other posttranscriptional modifications, methylation of different RNA species includes tRNA, rRNA, mRNA, tmRNA, snRNA, snoRNA, miRNA, and viral RNA. Different catalytic strategies are employed for RNA methylation by a variety of RNA-methyltransferases which fall into four superfamilies. This review outlines the different functions of methyl groups in RNA, including biophysical, biochemical and metabolic stabilization of RNA, quality control, resistance to antibiotics, mRNA reading frame maintenance, deciphering of normal and altered genetic code, selenocysteine incorporation,…

Models MolecularRNA methylationRNA-dependent RNA polymeraseRNA ArchaealBiologyMethylationBiochemistryRNA TransferDrug Resistance BacterialRNA Processing Post-TranscriptionalMolecular BiologyGeneticstRNA MethyltransferasesBinding SitesIntronRNANon-coding RNARNA BacterialRNA silencingRNA RibosomalRNA editingProtein BiosynthesisBiocatalysisNucleic Acid ConformationRNARNA ViralSmall nuclear RNAWIREs RNA
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Structures of Alkaloid Biosynthetic Glucosidases Decode Substrate Specificity

2011

Two similar enzymes with different biosynthetic function in one species have evolved to catalyze two distinct reactions. X-ray structures of both enzymes help reveal their most important differences. The Rauvolfia alkaloid biosynthetic network harbors two O-glucosidases: raucaffricine glucosidase (RG), which hydrolyses raucaffricine to an intermediate downstream in the ajmaline pathway, and strictosidine glucosidase (SG), which operates upstream. RG converts strictosidine, the substrate of SG, but SG does not accept raucaffricine. Now elucidation of crystal structures of RG, inactive RG-E186Q mutant, and its complexes with ligands dihydro-raucaffricine and secologanin reveals that it is the…

Models MolecularRauvolfiaStereochemistryIridoid GlucosidesMolecular Sequence DataMutantCrystallography X-RayBiochemistryRauwolfiaSubstrate SpecificityEvolution Molecularchemistry.chemical_compoundHydrolaseSerineAmino Acid SequenceVinca AlkaloidsPlant Proteinschemistry.chemical_classificationBinding SitesbiologyTryptophanSubstrate (chemistry)General Medicinebiology.organism_classificationKineticsEnzymechemistryBiochemistryStrictosidinebiology.proteinMolecular MedicineSecologaninGlucosidasesGlucosidasesProtein BindingACS Chemical Biology
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Participation of Two Ser-Ser-Phe-Tyr Repeats in Interleukin-6 (IL-6)-Binding Sites of the Human IL-6 Receptor

1996

The alpha-subunit of interleukin-6 (IL-6) receptor is a member of the hematopoietin receptor family. The alignment of its amino acid sequence with those of other members of this family (human somatotropin receptor/murine IL-3 receptor beta and human IL-2 receptor beta) has suggested that amino acids included in two SSFY repeats found in each of its hematopoietin receptor domains, contribute to the binding of the ligand. The involvement of these amino acids in IL-6 binding and signal transduction was studied by site-directed mutagenesis and molecular modelling. We present a computer-derived three-dimensional model of the IL-6/IL-6 receptor complex based on the structure of the human somatotr…

Models MolecularReceptor complexMolecular Sequence DataB-cell receptorInterleukin 5 receptor alpha subunitBiologyBiochemistryMiceAntigens CDTumor Cells CulturedEnzyme-linked receptorAnimalsHumans5-HT5A receptorAmino Acid SequenceNuclear receptor co-repressor 1Binding SitesBase SequenceInterleukin-6Antibodies MonoclonalReceptors InterleukinInterleukin-13 receptorReceptors Interleukin-6Molecular biologyBiochemistryMutationRabbitsEpitope MappingRelaxin/insulin-like family peptide receptor 2Signal TransductionEuropean Journal of Biochemistry
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Structural and Functional Similarity of Amphibian Constitutive Androstane Receptor with Mammalian Pregnane X Receptor

2016

The nuclear receptors and xenosensors constitutive androstane receptor (CAR, NR1I3) and pregnane X receptor (PXR, NR1I2) induce the expression of xenobiotic metabolizing enzymes and transporters, which also affects various endobiotics. While human and mouse CAR feature a high basal activity and low induction upon ligand exposure, we recently identified two constitutive androstane receptors in Xenopus laevis (xlCARá and â) that possess PXR-like characteristics such as low basal activity and activation in response to structurally diverse compounds. Using a set of complementary computational and biochemical approaches we provide evidence for xlCARá being the structural and functional counterpa…

Models MolecularReceptors SteroidReceptors Cytoplasmic and Nuclearlcsh:MedicineMolecular Dynamics SimulationPharmacologyBiologyCrystallography X-Raydigestive systemAmphibian ProteinsCell LineXenopus laevischemistry.chemical_compoundChlorocebus aethiopsConstitutive androstane receptorCoactivatorAnimalsHumansBinding sitelcsh:ScienceReceptorConstitutive Androstane ReceptorPregnane X receptorBinding SitesMultidisciplinarylcsh:RPregnane X ReceptorCorrectionLigand (biochemistry)digestive system diseasesCell biologychemistryNuclear receptorCOS Cellslcsh:QAndrostanePLOS ONE
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Topology and accessibility of the transmembrane helices and the sensory site in the bifunctional transporter DcuB of Escherichia coli.

2011

C(4)-Dicarboxylate uptake transporter B (DcuB) of Escherichia coli is a bifunctional transporter that catalyzes fumarate/succinate antiport and serves as a cosensor of the sensor kinase DcuS. Sites and domains of DcuB were analyzed for their topology relative to the cytoplasmic or periplasmic side of the membrane and their accessibility to the water space. For the topology studies, DcuB was fused at 33 sites to the reporter enzymes PhoA and LacZ that are only active when located in the periplasm or the cytoplasm, respectively. The ratios of the PhoA and LacZ activities suggested the presence of 10 or 11 hydrophilic loops, and 11 or 12 α-helical transmembrane domains (TMDs). The central part…

Models MolecularRecombinant Fusion ProteinsMolecular Sequence Datalac operonTopologyBiochemistryProtein Structure SecondaryPolyethylene GlycolsProtein structureBacterial ProteinsCatalytic DomainStilbenesAmino Acid SequenceCysteineBinding sitePeptide sequenceDicarboxylic Acid TransportersEscherichia coli K12ChemistryEscherichia coli ProteinsCell MembranePeriplasmic spaceAlkaline PhosphataseTransmembrane domainMembrane proteinBiochemistryLac OperonEthylmaleimideSulfonic AcidsHydrophobic and Hydrophilic InteractionsCysteineBiochemistry
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Electrostatic control of the photoisomerization efficiency and optical properties in visual pigments: on the role of counterion quenching.

2009

Hybrid QM(CASPT2//CASSCF/6-31G*)/MM(Amber) computations have been used to map the photoisomerization path of the retinal chromophore in Rhodopsin and explore the reasons behind the photoactivity efficiency and spectral control in the visual pigments. It is shown that while the electrostatic environment plays a central role in properly tuning the optical properties of the chromophore, it is also critical in biasing the ultrafast photochemical event: it controls the slope of the photoisomerization channel as well as the accessibility of the S(1)/S(0) crossing space triggering the ultrafast decay. The roles of the E113 counterion, the E181 residue, and the other amino acids of the protein pock…

Models MolecularRhodopsinPhotoisomerizationPhotochemistryStatic ElectricityPhotochemistryCrystallography X-RayBiochemistryCatalysisRetinaProtein environmentColloid and Surface ChemistryIsomerismAnimalschemistry.chemical_classificationIonsBinding SitesbiologyColor VisionComputational BiologyBiasingGeneral ChemistryChromophoreVisual pigmentschemistryRhodopsinMutationbiology.proteinQuantum TheoryThermodynamicsCattleCounterionProtonsUltrashort pulseJournal of the American Chemical Society
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Design and Synthesis of 4-Substituted Indolo[3,2-e][1,2,3]triazolo[1,5-a]pyrimidine Derivatives with Antitumor Activity

2008

New derivatives of the indolo[3,2- e][1,2,3]triazolo[1,5- a]pyrimidine system, substituted in the 4 position, were designed as novel antitumor agents because of their theoretical capability to form stable complexes with DNA fragments. The calculated free energies of binding were found in the range -12.76 --> -39.68 Kcal/mol. The docking studies revealed a common binding mode with the chromophore intercalated between GC base pairs, whereas the side chain lies along the minor groove. Compounds, selected on the basis of the docking studies and suitably synthesized, showed antiproliferative activity against each type of tumor cell line investigated, generally in the low micromolar range. The mo…

Models MolecularSEQUENCE SPECIFICITYMolecular modelPyrimidineStereochemistryDNA-BINDINGBIOLOGICAL INTERESTStereoisomerismAntineoplastic AgentsPyrimidinonesChemical synthesisHeterocyclic Compounds 4 or More RingsAUTOMATED DOCKINGchemistry.chemical_compoundStructure-Activity RelationshipCell Line TumorDrug DiscoveryStructure–activity relationshipHumansALGORITHMBinding siteCell ProliferationBinding SitesMolecular StructureChemistryBiological activityStereoisomerismDOMINO REACTIONDNADocking (molecular)Drug DesignNATIONAL-CANCER-INSTITUTEACTINOMYCIN-DMolecular MedicineCOMPLEXESDrug Screening Assays AntitumorTUMOR-CELL-LINES
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Structure-based analyses of Salmonella RcsB variants unravel new features of the Rcs regulon

2021

18 páginas, 7 figuras, 2 tablas

Models MolecularSalmonella typhimuriumIdentificationSignaling SystemTranscription GeneticTranscription FactorAcademicSubjects/SCI00010Protein ConformationProtein Data Bank (RCSB PDB)ExpressionBiologymedicine.disease_causeRegulonBiofilm Formation03 medical and health sciencesBacterial ProteinsCapsule SynthesisStructural BiologyGeneticsmedicineTranscriptional regulationPhosphorylationPromoter Regions GeneticTranscription factorGene030304 developmental biologyRegulation of gene expression0303 health sciencesMutationBinding Sites030306 microbiologyPromoterGene Expression Regulation BacterialBiología y Biomedicina / BiologíaRepressionCell biologyRegulonEscherichia-Coli K-12MutationGenome BacterialPhosphorelay SystemNucleic Acids Research
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A new approach to inhibit human β-tryptase by protein surface binding of four-armed peptide ligands with two different sets of arms

2013

A series of six new tetravalent ligands (1-6) with two different sets of arms bind to the surface of β-tryptase, a tetrameric enzyme with an A(2)B(2) arrangement of its four monomers and two different binding sites on its protein surface (as suggested by a docking study). Besides proteinogenic amino acids also the guanidiniocarbonyl pyrrole cation (abbreviated as GCP), as an artificial arginine analog, was introduced into the arms of the ligands to investigate its influence on protein surface binding and enzyme inhibition. Furthermore, four ligands (7-10) with four identical arms also containing the GCP group were additionally synthesized to study the influence of the GCP moiety on the inhi…

Models MolecularSerine Proteinase InhibitorsArginineStereochemistrySurface PropertiesChemieLigandsBiochemistryGuanidineschemistry.chemical_compoundStructure-Activity RelationshipMoietyHumansPyrrolesAmino Acid SequencePhysical and Theoretical ChemistryBinding sitechemistry.chemical_classificationBinding SitesMolecular StructureOrganic ChemistryLigand (biochemistry)Combinatorial chemistryAmino acidEnzymeMonomerchemistryDocking (molecular)TryptasesPeptidesBiologie
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A synthetic method for diversification of the P1′ substituent in phosphinic dipeptides as a tool for exploration of the specificity of the S1′ bindin…

2007

Abstract A novel, general, and versatile method of diversification of the P1′ position in phosphinic pseudodipeptides, presumable inhibitors of proteolytic enzymes, was elaborated. The procedure was based on parallel derivatization of the amino group in the suitably protected phosphinate building blocks with appropriate alkyl and aryl halides. This synthetic strategy represents an original approach to phosphinic dipeptide chemistry. Its usefulness was confirmed by obtaining a series of P1′ modified phosphinic dipeptides, inhibitors of cytosolic leucine aminopeptidase, through computer-aided design basing on the structure of homophenylalanyl-phenylalanine analogue (hPheP[CH 2 ]Phe) bound in …

Models MolecularStereochemistryClinical BiochemistryLAP inhibitorsSubstituentPharmaceutical SciencePhosphinateLigandsBiochemistryAminopeptidaseLeucyl AminopeptidaseStructure-Activity Relationshipchemistry.chemical_compoundDrug DiscoveryP1′ diversificationcross-couplingMolecular BiologyalkylationBinding SitesDipeptideMolecular StructurebiologyOrganic ChemistryProteolytic enzymesActive siteHydrogen BondingStereoisomerismDipeptidesPhosphinic Acidsphosphinic pseudodipeptideschemistrybiology.proteinMolecular MedicineLeucineLead compoundBioorganic & Medicinal Chemistry
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