Search results for "binding site"

showing 10 items of 856 documents

UV‐Vis Spectroscopy Reveals a Correlation Between Y263 and BV Protonation States in Bacteriophytochromes

2019

Red-light photosensory proteins, phytochromes, link light activation to biological functions by interconverting between two conformational states. For this, they undergo large-scale secondary and tertiary changes which follow small-scale Z to E bond photoisomerization of the covalently bound bilin chromophore. The complex network of amino acid interactions in the chromophore-binding pocket plays a central role in this process. Highly conserved Y263 and H290 have been found to be important for the photoconversion yield, while H260 has been identified as important for bilin protonation and proton transfer steps. Here, we focus on the roles these amino acids are playing in preserving the chemi…

Models Molecular0301 basic medicinePhotoisomerizationProtein ConformationStereochemistryProtonation010402 general chemistry01 natural sciencesBiochemistry03 medical and health scienceschemistry.chemical_compoundProtein structureMoleculeCloning MolecularPhysical and Theoretical ChemistryBilinchemistry.chemical_classificationBinding SitesPhytochromeSpectrum AnalysisGene Expression Regulation BacterialGeneral MedicineHydrogen-Ion ConcentrationChromophore0104 chemical sciencesAmino acid030104 developmental biologychemistryDeinococcusPhytochromePhotochemistry and Photobiology
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Transition state mimics are valuable mechanistic probes for structural studies with the arginine methyltransferase CARM1

2017

Coactivator associated arginine methyltransferase 1 (CARM1) is a member of the protein arginine methyltransferase (PRMT) family and methylates a range of proteins in eukaryotic cells. Overexpression of CARM1 is implicated in a number of cancers, and it is therefore seen as a potential therapeutic target. Peptide sequences derived from the well-defined CARM1 substrate poly(A)-binding protein 1 (PABP1) were covalently linked to an adenosine moiety as in the AdoMet cofactor to generate transition state mimics. These constructs were found to be potent CARM1 inhibitors and also formed stable complexes with the enzyme. High-resolution crystal structures of CARM1 in complex with these compounds co…

Models Molecular0301 basic medicineProtein-Arginine N-MethyltransferasesAdenosineMethyltransferaseCARM1ArgininePRMTCrystallography X-RayPoly(A)-Binding Protein ICofactorMice03 medical and health sciences0302 clinical medicineCatalytic DomainCoactivatorAnimalsAmino Acid Sequencetransition state mimicschemistry.chemical_classificationBinding SitesMultidisciplinarybiologycocrystal structuresActive siteProtein arginine N-methyltransferase; PRMT; CARM1; Transition state mimics; Cocrystal structuresMethylationBiological Sciencesprotein arginine N-methyltransferase030104 developmental biologyEnzymeCARM1chemistryBiochemistry030220 oncology & carcinogenesisbiology.proteinPeptidesProtein Binding
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Structure of the Human TRPML2 Ion Channel Extracytosolic/Lumenal Domain.

2019

Summary TRPML2 is the least structurally characterized mammalian transient receptor potential mucolipin ion channel. The TRPML family hallmark is a large extracytosolic/lumenal domain (ELD) between transmembrane helices S1 and S2. We present crystal structures of the tetrameric human TRPML2 ELD at pH 6.5 (2.0 A) and 4.5 (2.95 A), corresponding to the pH values in recycling endosomes and lysosomes. Isothermal titration calorimetry shows Ca2+ binding to the highly acidic central pre-pore loop which is abrogated at low pH, in line with a pH-dependent channel regulation model. Small angle X-ray scattering confirms the ELD dimensions in solution. Changes in pH or Ca2+ concentration do not affect…

Models Molecular0303 health sciencesBinding SitesTRPMLEndosomeChemistrySmall-angle X-ray scatteringProtein Conformation030302 biochemistry & molecular biologyIsothermal titration calorimetryHydrogen-Ion ConcentrationCrystallography X-Ray03 medical and health sciencesTransient receptor potential channelTransmembrane domainTransient Receptor Potential ChannelsProtein DomainsStructural BiologyBiophysicsHumansCalciumMolecular BiologyProtein secondary structureIon channel030304 developmental biologyStructure (London, England : 1993)
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Full Domain Closure of the Ligand-binding Core of the Ionotropic Glutamate Receptor iGluR5 Induced by the High Affinity Agonist Dysiherbaine and the …

2009

The prevailing structural model for ligand activation of ionotropic glutamate receptors posits that agonist efficacy arises from the stability and magnitude of induced domain closure in the ligand-binding core structure. Here we describe an exception to the correlation between ligand efficacy and domain closure. A weakly efficacious partial agonist of very low potency for homomeric iGluR5 kainate receptors, 8,9-dideoxyneodysiherbaine (MSVIII-19), induced a fully closed iGluR5 ligand-binding core. The degree of relative domain closure, approximately 30 degrees , was similar to that we resolved with the structurally related high affinity agonist dysiherbaine and to that of l-glutamate. The ph…

Models MolecularAgonistStereochemistrymedicine.drug_classGlutamic AcidKainate receptorCrystallography X-RayLigandsBiochemistryPartial agonistCell LineReceptors Kainic AcidmedicineHumansComputer SimulationAmino AcidsReceptorMolecular BiologyAlanineBinding SitesChemistryMechanisms of Signal TransductionGlutamate receptorHydrogen BondingCell BiologyBridged Bicyclo Compounds HeterocyclicLigand (biochemistry)Protein Structure TertiaryProtein SubunitsIonotropic glutamate receptorProtein BindingIonotropic effectJournal of Biological Chemistry
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Advances in DNA-ligands with groove binding, intercalating and/or alkylating activity: chemistry, DNA-binding and biology.

2005

It is known that DNA is a well-characterized intracellular target but its size and sequential characteristics make it an elusive target for selective drug action. Binding of low molecular weight ligands to DNA causes a variety of significant biological responses. In this context the main consideration is given to recent developments in DNA sequence selective binding agents bearing conjugated effectors because of their potential application in treatment of cancers, in diagnosis as well as in molecular biology. In the present review recent results about analogues of netropsins, distamycin A and of some lexitropsins and combilexins or related hybrid molecules with sequence reading, intercalati…

Models MolecularAlkylating AgentsMolecular modelLexitropsinLigandsBiochemistrychemistry.chemical_compoundDrug DiscoveryBinding sitePharmacologyBinding SitesPeptide nucleic acidbiologyMolecular StructureTopoisomeraseOrganic ChemistryNucleic acid sequenceDNAIntercalating AgentschemistryBiochemistryDrug DesignNucleic acidbiology.proteinMolecular MedicineNucleic Acid ConformationDNACurrent medicinal chemistry
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2,8-Diazido-ATP — a short-length bifunctional photoaffinity label for photoaffinity cross-linking of a stable F1 in ATP synthase (from thermophilic b…

1995

Abstract To demonstrate the direct interfacial position of nucleotide binding sites between subunits of proteins we have synthesized the bifunctional photoaffinity label 2,8-diazidoadenosine 5′-triphosphate (2,8-DiN3ATP). UV irradiation of the F1-ATPase (TF1) from the thermophilic bacterium PS3 in the presence of 2,8-DiN3ATP results in a nucleotide-dependent inactivation of the enzyme and in a nucleotide-dependent formation of α-β crosslinks. The results confirm an interfacial localization of all the nucleotide binding sites on TF1.

Models MolecularAzidesNucleotide binding siteLightStereochemistryImmunoblottingBiophysicsDirect interfacial localizationShort lengthBiochemistry8-azidoadenosine 5'-triphosphatechemistry.chemical_compoundAdenosine TriphosphateStructural BiologyGeneticsNucleotide binding sitesBifunctionalMolecular BiologyThermophilic bacterium PS3Photoaffinity cross-linkingchemistry.chemical_classificationATP synthasebiologyBacteriaThermophileAffinity LabelsCell BiologyProton-Translocating ATPasesEnzymeCross-Linking ReagentsBiochemistrychemistrybiology.proteinF1-ATPase: Short-length bifunctional photoaffinity labelFEBS Letters
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Site-by-site tracking of signal transduction in an azidophenylalanine-labeled bacteriophytochrome with step-scan FTIR spectroscopy

2021

Signal propagation in photosensory proteins is a complex and multidimensional event. Unraveling such mechanisms site-specifically in real time is an eligible but a challenging goal. Here, we elucidate the site-specific events in a red-light sensing phytochrome using the unnatural amino acid azidophenylalanine, vibrationally distinguishable from all other protein signals. In canonical phytochromes, signal transduction starts with isomerization of an excited bilin chromophore, initiating a multitude of processes in the photosensory unit of the protein, which eventually control the biochemical activity of the output domain, nanometers away from the chromophore. By implementing the label in pri…

Models MolecularAzidesProtein ConformationPhenylalaninespektroskopiaTongue regionGeneral Physics and Astronomyfotobiologia010402 general chemistryTracking (particle physics)01 natural sciences03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsSpectroscopy Fourier Transform InfraredAmino Acid SequenceAmino AcidsPhysical and Theoretical ChemistryFourier transform infrared spectroscopyBilin030304 developmental biology0303 health sciencesBinding SitesStaining and LabelingbiologyPhytochromeChemistryDeinococcus radioduransChromophorePhotochemical Processesbiology.organism_classification0104 chemical sciencesKineticsBiophysicsPhytochromeproteiinitvalokemiaSignal transductionProtein BindingSignal TransductionPhysical Chemistry Chemical Physics
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Dramatic selectivity differences in the association of DNA and RNA models with new ethylene- and propylene diamine derivatives and their copper compl…

2006

The affinities of polyamines consisting of ethylenediamine units equipped with either one or two terminal naphthyl-, anthryl-, or acridyl units towards PolyA.PolyU as an RNA model, and Poly(dA).Poly(dT) as a DNA model are screened by measuring the melting point changes (DeltaT(m)) of the double strands, and also partially by a fluorimetric binding assay using ethidium bromide. The larger aromatic moieties with long spacers between them allow bisintercalation; this leads to an increased preference for DNA in comparison to RNA, where ion pairing of the ammonium centers with the major RNA groove phosphates dominates. Allosteric affinity control by metalation is achieved e.g. with Cu(2+) ions, …

Models MolecularBinding SitesMetalationStereochemistryArylOrganic ChemistryRNAEthylenediamineDNADiaminesNucleic Acid DenaturationBiochemistryIntercalating Agentschemistry.chemical_compoundchemistryPoly dA-dTDiaminePoly A-URNAA-DNAPhysical and Theoretical ChemistryEthidium bromideDNACopperOrganicbiomolecular chemistry
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From Five- to Six-Membered Rings:  3,4-Diarylquinolinone as Lead for Novel p38MAP Kinase Inhibitors

2007

In this study we describe the design, synthesis, and biological evaluation of 3-(4-fluorophenyl)-4-pyridin-4-ylquinoline-2(1H)-one (5) as a new inhibitor of MAPK with a p38alphaMAPK IC50 of 1.8 muM. By keeping the common vicinal pyridine/4-F-phenyl pharmacophore, such as in prototypical imidazole 20 or isoxazole 13 but in 5 connected to the six-membered quinoline core, we were particularly interested in comparing biological activity, details of molecular geometry, and different binding modes of these compounds. Compounds 20 and 13 were active both in the p38alpha- and JNK3-assay, whereas 5 was selective for p38alpha, with no JNK3 inhibition. By comparing the X-ray structures of the compound…

Models MolecularBinding SitesMolecular modelStereochemistryQuinolineBiological activityQuinolonesCrystallography X-RayHeterocyclic Compounds 4 or More Ringsp38 Mitogen-Activated Protein KinasesStructure-Activity Relationshipchemistry.chemical_compoundchemistryMitogen-Activated Protein Kinase 10Drug DiscoveryPyridineMolecular MedicineImidazoleMoietyIsoxazolePharmacophoreJournal of Medicinal Chemistry
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Fractal-related assembly of the axial filament in the demosponge Suberites domuncula: relevance to biomineralization and the formation of biogenic si…

2007

Abstract The siliceous spicules of sponges (Porifera) show great variations of sizes, shapes and forms; they constitute the chief supporting framework of these animals; these skeletal elements are synthesized enzymatically by silicatein. Each sponge species synthesizes at least two silicateins, which are termed − α and − β . In the present study, using the demosponge Suberites domuncula , we studied if the silicateins of the axial filament contribute to the shape formation of the spicules. For these experiments native silicateins have been isolated by a new Tris/glycerol extraction procedure. Silicateins isolated by this procedure are monomeric (24 kDa), but readily form dimers through non-…

Models MolecularBiophysicsBioengineeringNanotechnologyBiomaterialsProtein filamentchemistry.chemical_compoundDemospongeSponge spiculeMicroscopy Electron TransmissionAnimalsAmino Acid SequenceCytoskeletonBinding SitesbiologyAnimal StructuresSilicon Dioxidebiology.organism_classificationImmunohistochemistryPoriferaSuberites domunculaSpongeFractalsMonomerchemistryMechanics of MaterialsCeramics and CompositesBiophysicsSelf-assemblyDimerizationBiomineralization
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