Search results for "binding site"

showing 10 items of 856 documents

Variations of acidic functions at position 2 and substituents at positions 4, 5 and 6 of the indole moiety and their effect on NMDA-glycine site affi…

2003

The synthetic procedures to obtain indole derivatives with different acidic functions at position 2 of the indole are reported. The synthesised and tested derivatives comprise 5-tetrazolyl, 1,3,4-oxadiazol-5-yl-2-one, and indole-2-carboxylic acid amides with 5-aminotetrazole, methanesulphonamide and trifluoromethanesulphonamide moieties. The binding affinity was evaluated using [3H]MDL 105,519 and pig cortical brain membranes. In general, compounds with acidic functions different from a carboxylic acid moiety are less potent than indole-2-carboxylic acid derivatives. Also, the 4,6-dichloro substitution pattern was compared to 5-tert-butyl derivatives and compounds not substituted in the ben…

Models MolecularIndolesSwineStereochemistryCarboxylic acidGlycineReceptors N-Methyl-D-AspartateChemical synthesisInhibitory Concentration 50Radioligand AssayStructure-Activity Relationshipchemistry.chemical_compoundDrug DiscoveryAnimalsMoietyBenzeneImideCerebral CortexPharmacologyIndole testchemistry.chemical_classificationBinding SitesBicyclic moleculeCell MembraneOrganic ChemistryGeneral MedicineLigand (biochemistry)MembranechemistryGlycineHydantoin derivativesNMDA receptorEuropean Journal of Medicinal Chemistry
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Design, Synthesis, and Biological Evaluation of 3,4-Diarylmaleimides as Angiogenesis Inhibitors

2006

The new analogue 2 of combretastatin A-4 was discovered to be an inhibitor of tubulin polymerization with an IC50 of 7.6 microM and reduced angiogenesis in the in vivo chick embryo model. Interestingly, in a series of 2,3-diarylmaleimides closely related to this lead, no other compound was found to be active in the tubulin polymerization assay. However, by screening in the in vivo chick embryo assay 10 was identified as a potent angiogenesis inhibitor indicating an alternative target. Indeed, molecular modeling studies suggest a reasonable binding mode of 10 at the ATP-binding site of the model kinase CDK2. Motivated by these results, analogues of 10 were screened for inhibitory activity in…

Models MolecularIndolesanimal structuresAngiogenesisAngiogenesis InhibitorsChick EmbryoIn Vitro TechniquesMaleimidesStructure-Activity Relationshipchemistry.chemical_compoundAdenosine TriphosphateIn vivoDrug DiscoveryAnimalsStructure–activity relationshipPyrrolesBinding siteCombretastatinBinding SitesbiologyChemistryKinaseCyclin-dependent kinase 2Vascular Endothelial Growth Factor Receptor-2Angiogenesis inhibitorBiochemistryDrug Designbiology.proteinMolecular MedicineJournal of Medicinal Chemistry
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Molecular dynamics simulation of sucrose- and trehalose-coated carboxy-myoglobin

2005

We performed a room temperature molecular dynamics (MD) simulation on a system containing 1 carboxy-myoglobin (MbCO) molecule in a sucrose–water matrix of identical composition (89% [sucrose/(sucrose + water)] w/w) as for a previous trehalose–water–MbCO simulation (Cottone et al., Biophys J 2001;80:931–938). Results show that, as for trehalose, the amplitude of protein atomic mean-square fluctuations, on the nanosecond timescale, is reduced with respect to aqueous solutions also in sucrose. A detailed comparison as a function of residue number evidences mobility differences along the protein backbone, which can be related to a different efficacy in bioprotection. Different heme pocket struc…

Models MolecularInfrared spectroscopyDisaccharidesBiochemistrychemistry.chemical_compoundMolecular dynamicsStructural BiologyCarbohydrate ConformationMoleculeComputer Simulationheme pocket; hydrogen bond; mean-square fluctuations; protein dynamics; sucrose; trehaloseheme pocketMolecular Biologytrehalosehydrogen bondAqueous solutionBinding SitesHydrogen bondMyoglobinProtein dynamicssucroseTrehaloseCrystallographyKineticschemistryMyoglobinprotein dynamicsmolecular dynamics myoglobin disaccharidemean-square fluctuations
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"RKKH" peptides from the snake venom metalloproteinase of Bothrops jararaca bind near the metal ion-dependent adhesion site of the human integrin alp…

1999

Integrin alpha(1)beta(1) and alpha(2)beta(1) are the major cellular receptors for collagen, and collagens bind to these integrins at the inserted I-domain in their alpha subunit. We have previously shown that a cyclic peptide derived from the metalloproteinase domain of the snake venom protein jararhagin blocks the collagen-binding function of the alpha(2) I-domain. Here, we have optimized the structure of the peptide and identified the site where the peptide binds to the alpha(2) I-domain. The peptide sequence Arg-Lys-Lys-His is critical for recognition by the I-domain, and five negatively charged residues surrounding the "metal ion-dependent adhesion site" (MIDAS) of the I-domain, when mu…

Models MolecularIntegrinsReceptors CollagenIntegrinMolecular Sequence DataIntegrin alpha2PeptidePeptide bindingBiochemistryAntigens CDCrotalid VenomsAnimalsHumansBothropsComputer SimulationAmino Acid SequenceMolecular BiologyPeptide sequencechemistry.chemical_classificationMetalloproteinaseBinding SitesbiologySequence Homology Amino AcidChemistryActive siteMetalloendopeptidasesCell BiologyCyclic peptidePeptide FragmentsCell biologyBiochemistryJararhaginbiology.proteinMutagenesis Site-DirectedCell Adhesion MoleculesProtein BindingThe Journal of biological chemistry
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Structure of three tandem filamin domains reveals auto-inhibition of ligand binding

2007

Human filamins are large actin-crosslinking proteins composed of an N-terminal actin-binding domain followed by 24 Ig-like domains (IgFLNs), which interact with numerous transmembrane receptors and cytosolic signaling proteins. Here we report the 2.5 A resolution structure of a three-domain fragment of human filamin A (IgFLNa19-21). The structure reveals an unexpected domain arrangement, with IgFLNa20 partially unfolded bringing IgFLNa21 into close proximity to IgFLNa19. Notably the N-terminus of IgFLNa20 forms a beta-strand that associates with the CD face of IgFLNa21 and occupies the binding site for integrin adhesion receptors. Disruption of this IgFLNa20-IgFLNa21 interaction enhances fi…

Models MolecularIntegrinsanimal structuresintegrinFilaminsIntegrinmacromolecular substancesPlasma protein bindingLigandsFilaminBiochemistryArticleGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciencesFilamin bindingContractile ProteinsHumansBinding siteCell adhesionCytoskeletonMolecular BiologyX-ray crystallography030304 developmental biologyIntegrin binding0303 health sciencesGeneral Immunology and MicrobiologybiologyGeneral NeuroscienceMicrofilament Proteins030302 biochemistry & molecular biologycell adhesioncytoskeletonfilaminProtein Structure TertiaryCell biologybiology.proteinProtein BindingThe EMBO Journal
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Electrochemical detection of the 2-isobutyl-3-methoxypyrazine model odorant based on odorant-binding proteins: The proof of concept

2014

Abstract We developed an electrochemical assay for the detection of odorant molecules based on a rat odorant-binding protein (rOBP3). We demonstrated that rOBP3 cavity binds 2-methyl-1,4-naphtoquinone (MNQ), an electrochemical probe, as depicted from the decrease of its electrochemical signal, and deduced the dissociation constant, Kd MNQ  = 0.5(± 0.2) μM. The amount of MNQ displaced from rOBP3 by 2-isobutyl-3-methoxypyrazine (IBMP), a model odorant molecule, was measured using square-wave voltammetry. The release of MNQ by competition led to an increase of the electrochemical response. In addition, this method allowed determination of the dissociation constant of rOBP3 for IBMP, Kd IBMP  =…

Models MolecularIsothermal microcalorimetryOdorant bindingBiophysicsAnalytical chemistryCalorimetryReceptors OdorantElectrochemistryBinding CompetitiveCaffeic AcidsElectrochemistryPhysical and Theoretical ChemistryVoltammetryBinding SitesChemistryVitamin K 3Electrochemical TechniquesGeneral MedicineCombinatorial chemistryFluorescenceRecombinant ProteinsDissociation constantImmobilized ProteinsSpectrometry FluorescencePyrazinesCalibrationTitrationBiosensorBioelectrochemistry
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Nuclear magnetic resonance spectroscopic study of beta-lactoglobulin interactions with two flavor compounds, gamma-decalactone and beta-ionone.

2002

Interactions between a well-characterized protein, beta-lactoglobulin, and two flavor compounds, beta-ionone and gamma-decalactone, were studied by 2D NMR spectroscopy. NMR spectra were recorded in aqueous solution (pH 2.0, 12 mM NaCl, 10% D(2)O) under conditions such that beta-lactoglobulin is present in a monomeric state. TOCSY and NOESY spectra were recorded on the protein and the complexes between protein and ligands. The spectra of the NH-CH(alpha) region showed the cross-signals due to the coupling between N- and C-bonded protons in the polypeptide backbone. The observed chemical shift variations in the presence of ligands can be assigned to changes in the protein conformation. It app…

Models MolecularKetoneMagnetic Resonance SpectroscopyStereochemistryProtein ConformationLactoglobulinsIononechemistry.chemical_compoundLactonesSpectroscopyBeta-lactoglobulinFlavorchemistry.chemical_classificationBinding SitesbiologyMolecular StructureTerpenesGeneral ChemistryNuclear magnetic resonance spectroscopyNMR spectra databasechemistryOdorantsbiology.proteinPhysical chemistryGeneral Agricultural and Biological SciencesNorisoprenoidsTwo-dimensional nuclear magnetic resonance spectroscopyJournal of agricultural and food chemistry
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Signal amplification and transduction in phytochrome photosensors

2014

[Introduction] Page 2 of 20 Sensory proteins must relay structural signals from the sensory site over large distances to regulatory output domains. Phytochromes are a major family of red-light sensing kinases that control diverse cell ular functions in plants, bacteria, and fungi. 1-9 Bacterial phytochro mes consist of a photosensory core and a C-te rminal regulatory domain. 10,11 Structures of photosensory cores are reported in the resting state 12-18 and conformational responses to light activat ion have been proposed in the vicinity of the chromophore. 19-23 However, the structure of the signalling state and the mechanism of downstream signal re lay through the photosensory core remain e…

Models MolecularLight Signal TransductionProtein ConformationCrystallography X-RayArticleProtein structureBacterial Proteinsmolecular biophysicsDeinococcusBinding siteCalcium signalingBinding SitesMultidisciplinarybiokemiabiologyPhytochrometa1182Deinococcus radioduransChromophorebiology.organism_classificationBiochemistryBiophysicsDeinococcusPhytochromeTransduction (physiology)röntgenkristallografiaNature
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Structural determinants of resveratrol for cell proliferation inhibition potency: experimental and docking studies of new analogs.

2010

International audience; Resveratrol is the subject of intense research because of the abundance of this compound in the human diet and as one of the most valuable natural chemopreventive agents. Further advances require new resveratrol analogs be used to identify the structural determinants of resveratrol for the inhibition potency of cell proliferation by comparing experimental and docking studies. Therefore, we synthesized new trans/(E)- and cis/(Z)-resveratrol - analogs not reported to date - by modifying the hydroxylation pattern of resveratrol and a double bond geometry. We included them in a larger panel of 14 molecules, including (Z)-3,5,4'-trimethoxystilbene, the most powerful molec…

Models MolecularMESH : HydroxidesMESH : DNAMESH: Cell CycleMESH: TubulinResveratrolHydroxylationchemistry.chemical_compound0302 clinical medicineTubulinMESH: StilbenesDrug DiscoveryStilbenesHydroxidesMESH : Cell ProliferationDocking studiesMESH : Colchicine0303 health sciencesCell CycleMESH: DNAStereoisomerismGeneral MedicineMESH : TubulinMESH: Hydroxides3. Good healthColon cancerBiochemistryMESH : Stereoisomerism030220 oncology & carcinogenesisMESH: Models MolecularMESH: Cell Line TumorStereochemistryMESH : Models MolecularStereoisomerismMESH : Stilbenes03 medical and health sciencesCell Line TumorMESH: Cell ProliferationMESH : Cell Cycle[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyHumans[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyBinding site[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyTubulin polymerization030304 developmental biologyCell ProliferationPharmacologyCombretastatinBinding SitesMESH: HumansCell growthMESH : Cell Line TumorOrganic ChemistryMESH : HumansDNAMESH: StereoisomerismMESH: ColchicinechemistryPolymethoxy-stilbenesMESH: Binding SitesDocking (molecular)Cell cultureResveratrolResveratrol; Polymethoxy-stilbenes; Tubulin polymerization; Colon cancer; Docking studiesColchicineMESH : Binding Sites
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Effects of static and dynamic perturbations on isotropic hyperfine coupling constants in some quinone radicals.

2004

The effects of solvent dielectric response on the isotropic hyperfine coupling constants of the 1,4-benzoquinone, 1,4-naphthoquinone and 9,10-anthraquinone anions and 1,4-naphthalenediol cation radicals were studied by electron spin resonance (ESR) spectroscopy and by the theoretical density functional method within the polarizable continuum model. Experimental results demonstrate that the isotropic hyperfine coupling constants can be obtained with high accuracy and that the effects of solvent impurities can be minimized by careful sample preparation. The results obtained correlate well with theoretical predictions from density functional theory calculations. For 1,4-naphthalenediol both th…

Models MolecularMagnetic Resonance SpectroscopyFree RadicalsRadicalMolecular ConformationPolarizable continuum modelMolecular physicsSensitivity and Specificitylaw.inventionlawImpurityComputational chemistryElectric ImpedanceGeneral Materials ScienceComputer SimulationSpectroscopyElectron paramagnetic resonanceBinding SitesChemistryIsotropyQuinonesReproducibility of ResultsGeneral ChemistrySolventKineticsSolventsAnisotropyDensity functional theoryArtifactsMagnetic resonance in chemistry : MRC
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