Search results for "binding site"

showing 10 items of 856 documents

Tarantula Hemocyanin Shows Phenoloxidase Activity

1998

An enzyme generally catalyzes one well defined reaction with high specificity and efficiency. We report here in contrast that the copper protein hemocyanin of the tarantula Eurypelma californicum exhibits two different functions. These occur at the same active site. While hemocyanin usually is an oxygen carrier, its function can be transformed totally to monophenoloxidase and o-diphenoloxidase activity after limited proteolysis with trypsin or chymotrypsin. N-acetyldopamine (NADA) is more effectively oxidized than L-dopa or dopamine. This irreversible functional switch of tarantula hemocyanin function is limited to the two subunits b and c of its seven subunit types. A conserved phenylalani…

Models MolecularStereochemistryCopper proteinDopamineProtein subunitmedicine.medical_treatmentPhenylalanineBiochemistrySubstrate SpecificityLevodopaMetalloproteinsMetalloproteinmedicineAnimalsChymotrypsinTrypsinImmunoelectrophoresisMolecular Biologychemistry.chemical_classificationBinding SitesbiologyMonophenol MonooxygenaseActive siteSpidersHemocyaninCell BiologyTrypsinOxygenEnzymeBiochemistrychemistrySpectrophotometryHemocyaninsbiology.proteinElectrophoresis Polyacrylamide GelCoppermedicine.drugJournal of Biological Chemistry
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N-(INDAZOLYL)BENZAMIDO DERIVATIVES AS CDK1 INHIBITORS: DESIGN, SYNTHESIS, BIOLOGICAL ACTIVITY, AND MOLECULAR DOCKING STUDIES

2009

A series of N-1H-indazole-1-carboxamides has been synthesized and their effects on both CDK1/cyclin B and the K-562 (human chronic myelogenus leukemia) cell line were evaluated. Using a computational model, we have observed that all the most active compounds 9e, f, i-n exhibited the same binding mode of purvanalol A in the ATP-binding cleft. Although they were able to moderately inhibit the leukemic cell line K-562 and to show inhibitory activity against the Cdc2-Cyclin B kinase in the low micromolar range, they turned out to be non-cytotoxic against HuDe (IZSL) primary cell cultures from human derm. These preliminary results are quite encouraging in view of the low toxicity demonstrated by…

Models MolecularStereochemistryCyclin BPharmaceutical ScienceAntineoplastic AgentsCyclin BStructure-Activity RelationshipCDC2 Protein KinaseDrug DiscoveryHumansStructure–activity relationshipCell ProliferationCyclin-dependent kinase 1Binding SitesbiologyCell growthChemistryImidazolesN-(1H-indazolyl)benzamides 1H-indazole-3-carboxamides CDK1 Molecular dockingBiological activitySettore CHIM/08 - Chimica FarmaceuticaBiochemistryDocking (molecular)Cell cultureDrug DesignBenzamidesbiology.proteinDrug Screening Assays AntitumorK562 CellsCDC2 Protein KinaseProtein Binding
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Ligand structures of synthetic deoxa-pyranosylamines with raucaffricine and strictosidine glucosidases provide structural insights into their binding…

2014

Insight into the structure and inhibition mechanism of O-β-d-glucosidases by deoxa-pyranosylamine type inhibitors is provided by X-ray analysis of complexes between raucaffricine and strictosidine glucosidases and N-(cyclohexylmethyl)-, N-(cyclohexyl)- and N-(bromobenzyl)-β-d-gluco-1,5-deoxa-pyranosylamine. All inhibitors anchored exclusively in the catalytic active site by competition with appropriate enzyme substrates. Thus facilitated prospective elucidation of the binding networks with residues located at <3.9 A distance will enable the development of potent inhibitors suitable for the production of valuable alkaloid glucosides, raucaffricine and strictosidine, by means of synthesis in …

Models MolecularStereochemistryCyclopentanesLigandsRauwolfiaStructure-Activity RelationshipSugar AlcoholsRauvolfia serpentinaDrug DiscoveryHydrolasePharmacologychemistry.chemical_classificationBinding SitesDose-Response Relationship DrugMolecular StructurebiologyAlkaloidActive siteGeneral Medicinebiology.organism_classificationLigand (biochemistry)EnzymeBiochemistrychemistryStrictosidinebiology.proteinGlucosidasesGlucosidasesJournal of Enzyme Inhibition and Medicinal Chemistry
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Inside the Hsp90 inhibitors binding mode through induced fit docking

2009

Abstract During the last few decades, the development of new anticancer strategies had to face the instability of many tumors, occurring when the genetic plasticity of cells produces new drug-resistant cancers. It has been shown that a chaperone protein, heat shock protein 90 (Hsp90), is one of the fundamental factors involved in the cell response to stresses, and its role in many biochemical pathways has been demonstrated. Thus, the inhibition of Hsp90 represents a new target of antitumor therapy, since it may influence many specific signaling pathways. The natural antibiotic Geldanamycin is the first Hsp90 inhibitor that has been identified. Nevertheless, more potent and water-soluble sma…

Models MolecularStereochemistryLactams MacrocyclicMolecular Sequence DataComputational biologyCrystallography X-RayLigandsHsp90 inhibitorchemistry.chemical_compoundAdenosine TriphosphateHeat shock proteinCatalytic DomainMaterials ChemistryBenzoquinonesAmino Acid SequenceHSP90 Heat-Shock ProteinsPhysical and Theoretical ChemistrySpectroscopyInduced fitBinding SitesbiologyMolecular StructureHeat shock proteinDrug discoveryActive siteGeldanamycinRadicicolComputer Graphics and Computer-Aided DesignSmall moleculeHsp90Settore CHIM/08 - Chimica FarmaceuticachemistryDocking (molecular)Molecular dockingbiology.proteinGeldanamicynSequence AlignmentProtein Binding
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Dibutyltin(IV) complexes containing arylazobenzoate ligands: chemistry, in vitro cytotoxic effects on human tumor cell lines and mode of interaction …

2009

Dibutyltin(IV) complexes of composition Bu2Sn (LH)2, where LH is a carboxylate residue derived from 2-[(E)- (5-tert-butyl-2- hydroxyphenyl)diazenyl]benzoate (L1H) with water molecule (1), 4-[(E)-(5-tert-butyl-2-hydroxyphenyl) diazenyl]benzoate (L2H) (2) and 4-[(E)-(4-hydroxy-5- methylphenyl)diazenyl]benzoate (L3H) (3), were synthesized and characterized by spectroscopic (1H, 13C and 119Sn NMR, IR, 119Sn Mössbauer) techniques. A full characterization was accomplished from the crystal structure of complex 1. The molecular structures and geometries of the complexes (1a i.e. 1 without water molecule and 3) were fully optimized using the quantum mechanical method (PM6). Complexes 1 and 3 were fo…

Models MolecularStereochemistryMolecular ConformationCrystallography X-RayLigandsThymidylate synthaseAnti-cancer drugchemistry.chemical_compoundCell Line TumorRibonucleotide ReductasesOrganotin CompoundsMoleculeHumansPharmacology (medical)CarboxylateArylazobenzoateSpectroscopyPharmacologychemistry.chemical_classificationBinding SitesbiologyCell DeathTopoisomeraseHydrogen BondingThymidylate SynthaseIn vitroEnzymesRibonucleotide reductaseEnzymeDNA Topoisomerases Type IIOncologychemistrySettore CHIM/03 - Chimica Generale E InorganicaDocking (molecular)Docking studieDibutyltin(IV) compoundbiology.proteinQuantum TheoryDrug Screening Assays AntitumorCell lineInvestigational new drugs
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The 1.45 A resolution structure of the cryptogein-cholesterol complex: a close-up view of a sterol carrier protein (SCP) active site.

2002

Cryptogein is a small 10 kDa elicitor produced by the phytoparasitic oomycete Phytophthora cryptogea. The protein also displays a sterol carrier activity. The native protein crystallizes in space group P4(1)22, with unit-cell parameters a = b = 46.51, c = 134.9 A (diffraction limit: 2.1 A). Its complex with cholesterol crystallizes in space group C222(1), with unit-cell parameters a = 30.96, b = 94.8, c = 65.3 A and a resolution enhanced to 1.45 A. The large inner non-specific hydrophobic cavity is able to accommodate a large variety of 3-beta-hydroxy sterols. Cryptogein probably acts as a sterol shuttle helping the pathogen to grow and complete its life cycle.

Models MolecularStereochemistryMolecular Sequence DataBiologyFungal Proteinschemistry.chemical_compoundStructural BiologyAmino Acid SequenceOomyceteBinding SitesMolecular StructureSequence Homology Amino AcidCholesterolPhytophthora cryptogeaResolution (electron density)Algal ProteinsActive siteGeneral Medicinebiology.organism_classificationSterolElicitorSterolsSterol carrier proteinCholesterolBiochemistrychemistrybiology.proteinCarrier ProteinsActa crystallographica. Section D, Biological crystallography
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High Pressure Enhances Hexacoordination in Neuroglobin and Other Globins

2005

The techniques of high applied pressure and flash photolysis have been combined to study ligand rebinding to neuroglobin (Ngb) and tomato Hb, globins that may display a His-Fe-His hexacoordination in the absence of external ligands. High pressure induces a moderate decrease in the His association rate and a large decrease in His dissociation rate, thus leading to an enhancement of the overall His affinity. The overall structural difference between penta- and hexacoordinated globins may be rather small and can be overcome by external modifications such as high pressure. Over the pressure range 0.1-700 MPa (7 kbar), the globins may show a loss of over a factor of 100 in the amplitude of the b…

Models MolecularSteric effectsProtein ConformationStereochemistryIronNeuroglobinchemistry.chemical_elementNerve Tissue ProteinsHemeLigandsBiochemistryOxygenHemoglobinschemistry.chemical_compoundSolanum lycopersicumPressureAnimalsHumansHistidineHorsesGlobinMolecular BiologyHemeBinding SitesPhotolysisMyoglobinChemistryPhotodissociationHeartCell BiologyLigand (biochemistry)GlobinsOxygenKineticsNeuroglobinBiophysicsFlash photolysisProtein BindingJournal of Biological Chemistry
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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
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Molecular Architecture of Strictosidine Glucosidase: The Gateway to the Biosynthesis of the Monoterpenoid Indole Alkaloid Family[W]

2007

Abstract Strictosidine β-d-glucosidase (SG) follows strictosidine synthase (STR1) in the production of the reactive intermediate required for the formation of the large family of monoterpenoid indole alkaloids in plants. This family is composed of ∼2000 structurally diverse compounds. SG plays an important role in the plant cell by activating the glucoside strictosidine and allowing it to enter the multiple indole alkaloid pathways. Here, we report detailed three-dimensional information describing both native SG and the complex of its inactive mutant Glu207Gln with the substrate strictosidine, thus providing a structural characterization of substrate binding and identifying the amino acids …

Models MolecularStrictosidine synthaseGlutamineGlutamic AcidPlant ScienceCrystallography X-RayLigandsCatalysisProtein Structure SecondaryRauwolfiaIndole AlkaloidsSubstrate Specificitychemistry.chemical_compoundBiosynthesisHydrolaseVinca AlkaloidsResearch ArticlesBinding SitesbiologyATP synthaseIndole alkaloidActive siteCell BiologySecologanin Tryptamine AlkaloidsKineticsBiochemistrychemistryStrictosidinebiology.proteinMutagenesis Site-DirectedMutant ProteinsGlucosidasesGlucosidases
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Synthesis, in vitro activity, and three-dimensional quantitative structure-activity relationship of novel hydrazine inhibitors of human vascular adhe…

2010

Vascular adhesion protein-1 (VAP-1) belongs to the semicarbazide-sensitive amine oxidases (SSAOs) that convert amines into aldehydes. SSAOs are distinct from the mammalian monoamine oxidases (MAOs), but their substrate specificities are partly overlapping. VAP-1 has been proposed as a target for anti-inflammatory drug therapy because of its role in leukocyte adhesion to endothelium. Here, we describe the synthesis and in vitro activities of novel series of VAP-1 selective inhibitors. In addition, the molecular dynamics simulations performed for VAP-1 reveal that the movements of Met211, Ser496, and especially Leu469 can enlarge the ligand-binding pocket, allowing larger ligands than those s…

Models MolecularSubstrate SpecificitiesQuantitative structure–activity relationshipMolecular ConformationQuantitative Structure-Activity RelationshipMolecular Dynamics SimulationLigandsMolecular dynamicsCricetulusCricetinaeDrug DiscoveryAnimalsHumansMonoamine OxidaseBinding SitesChemistryStereoisomerismIn vitrorespiratory tract diseasesRatsMonoamine neurotransmitterHydrazinesBiochemistryDocking (molecular)Molecular MedicineAmine gas treatingAmine Oxidase (Copper-Containing)Cell Adhesion MoleculesVASCULAR ADHESION PROTEIN 1Protein BindingJournal of medicinal chemistry
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