Search results for "Biomacromolecule-Ligand Interactions"

showing 10 items of 12 documents

Structural Mechanism of N-Methyl-D-Aspartate Receptor Type 1 Partial Agonism

2012

N-methyl-D-aspartate (NMDA) receptors belong to a family of ionotropic glutamate receptors that contribute to the signal transmission in the central nervous system. NMDA receptors are heterotetramers that usually consist of two GluN1 and GluN2 monomers. The extracellular ligand-binding domain (LBD) of a monomer is comprised of discontinuous segments that form the functional domains D1 and D2. While the binding of a full agonist glycine to LBD of GluN1 is linked to cleft closure and subsequent ion-channel opening, partial agonists are known to activate the receptor only sub-maximally. Although the crystal structures of the LBD of related GluA2 receptor explain the mechanism for the partial a…

AgonistProtein Structuremedicine.drug_classGlycineMolecular ConformationBiophysicslcsh:MedicineMolecular Dynamics SimulationLigandsta3111Receptors N-Methyl-D-AspartateBiochemistryBiophysics Simulationsta3112Partial agonistIon ChannelsChemical BiologyMacromolecular Structure AnalysismedicineBiomacromolecule-Ligand Interactionslcsh:ScienceReceptorBiologyta116Ion channelCrystallographyMultidisciplinaryChemistrylcsh:Rta1182Glutamate receptorProteinsComputational BiologyNeurotransmittersProtein Structure TertiaryTransmembrane ProteinsBiochemistryCycloserineBiophysicsNMDA receptorLigand-gated ion channellcsh:Qhormones hormone substitutes and hormone antagonistsProtein BindingResearch ArticleNeuroscienceIonotropic effectPLoS ONE
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Shared midgut binding sites for Cry1A.105, Cry1Aa, Cry1Ab, Cry1Ac and Cry1Fa proteins from Bacillus thuringiensis in two important corn pests, Ostrin…

2013

First generation of insect-protected transgenic corn (Bt-corn) was based on the expression of Cry1Ab or Cry1Fa proteins. Currently, the trend is the combination of two or more genes expressing proteins that bind to different targets. In addition to broadening the spectrum of action, this strategy helps to delay the evolution of resistance in exposed insect populations. One of such examples is the combination of Cry1A.105 with Cry1Fa and Cry2Ab to control O. nubilalis and S. frugiperda. Cry1A.105 is a chimeric protein with domains I and II and the C-terminal half of the protein from Cry1Ac, and domain III almost identical to Cry1Fa. The aim of the present study was to determine whether the c…

Agricultural BiotechnologyApplied MicrobiologyCoated vesiclePlant SciencePlasma protein bindingMothsBiochemistryOstriniaPlagues ControlBacillus thuringiensisBiomacromolecule-Ligand InteractionsPlant PestsMultidisciplinaryMicrovillibiologyGenetically Modified OrganismsQRAgricultureRecombinant ProteinsBiochemistryLarvaMedicineDisease SusceptibilityAgrochemicalsResearch ArticleBiotechnologyProtein BindingScienceProtein domainBiotecnologia agrícolaBacillus thuringiensisCoated VesiclesCerealsCropsSpodopteraSpodopteraMicrobiologyBinding CompetitiveZea maysBacterial ProteinsBotanyAnimalsPesticidesBinding siteProtein InteractionsBiologyTransgenic PlantsfungiProteinsPlant Pathologybiology.organism_classificationFusion proteinMaizeGastrointestinal TractKineticsPlant BiotechnologyPest ControlProteïnes
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Gray Matter NG2 Cells Display Multiple Ca2+-Signaling Pathways and Highly Motile Processes

2011

NG2 cells, the fourth type of glia in the mammalian CNS, receive synaptic input from neurons. The function of this innervation is unknown yet. Postsynaptic changes in intracellular Ca(2+)-concentration ([Ca(2+)](i)) might be a possible consequence. We employed transgenic mice with fluorescently labeled NG2 cells to address this issue. To identify Ca(2+)-signaling pathways we combined patch-clamp recordings, Ca(2+)-imaging, mRNA-transcript analysis and focal pressure-application of various substances to identified NG2-cells in acute hippocampal slices. We show that activation of voltage-gated Ca(2+)-channels, Ca(2+)-permeable AMPA-receptors, and group I metabotropic glutamate-receptors provo…

Central Nervous SystemAnatomy and PhysiologyVesicular glutamate transporter 1Glycobiologylcsh:MedicineHippocampal formationBiochemistryIon ChannelsTransmembrane Transport ProteinsMice0302 clinical medicinePostsynaptic potentialBiomacromolecule-Ligand Interactionslcsh:ScienceCells CulturedMembrane potential0303 health sciencesMultidisciplinarybiologyReverse Transcriptase Polymerase Chain ReactionDepolarizationNeurochemistryNeurotransmittersCell biologyElectrophysiologymedicine.anatomical_structureNeurologyNeurogliaMedicineProteoglycansNeurochemicalsGlutamateNeurogliaResearch ArticleNervous System PhysiologySignal TransductionCell PhysiologyMotilityNeuroimagingMice TransgenicNeurological System03 medical and health sciencesNeuropharmacologymedicineAnimalsHumansddc:610Biology030304 developmental biologyEndoplasmic reticulumlcsh:RProteinsGamma-Aminobutyric AcidTransmembrane ProteinsLuminescent ProteinsMicroscopy Electronnervous systemMicroscopy FluorescenceSynapsesVesicular Glutamate Transport Protein 1biology.proteinNervous System Componentslcsh:QCalciumPhysiological Processes030217 neurology & neurosurgeryNeurosciencePLoS ONE
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The Bile Acid Receptor GPBAR-1 (TGR5) Modulates Integrity of Intestinal Barrier and Immune Response to Experimental Colitis

2011

Background GP-BAR1, a member G protein coupled receptor superfamily, is a cell surface bile acid-activated receptor highly expressed in the ileum and colon. In monocytes, ligation of GP-BAR1 by secondary bile acids results in a cAMP-dependent attenuation of cytokine generation. Aims To investigate the role GP-BAR1 in regulating intestinal homeostasis and inflammation-driven immune dysfunction in rodent models of colitis. Methods Colitis was induced in wild type and GP-BAR1−/− mice by DSS and TNBS administration. Potential GP-BAR1 agonists were identified by in silico screening and computational docking studies. Results GP-BAR1−/− mice develop an abnormal morphology of colonic mucous cells a…

Cholera ToxinCD14Biophysicslcsh:MedicineInflammationGastroenterology and HepatologyBiologyLigandsBiochemistryPermeabilityReceptors G-Protein-CoupledTight JunctionsMiceCrohn DiseaseCiprofloxacinMolecular Cell BiologymedicineAnimalsUlcerative ColitisIntestinal MucosaProtein PrecursorsBiomacromolecule-Ligand InteractionsColitislcsh:ScienceReceptorBiologyMice KnockoutMultidisciplinaryIntestinal permeabilityHaptoglobinsPhysicsInflammatory Bowel Diseaselcsh:RImmunityZonulinColitisFlow Cytometrymedicine.diseaseMolecular biologyG protein-coupled bile acid receptorImmunologyTLR4Medicinelcsh:Qmedicine.symptomCytometryResearch ArticlePLoS ONE
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CO rebinding kinetics and molecular dynamics simulations highlight dynamic regulation of internal cavities in human cytoglobin

2013

Abstract: Cytoglobin (Cygb) was recently discovered in the human genome and localized in different tissues. It was suggested to play tissue-specific protective roles, spanning from scavenging of reactive oxygen species in neurons to supplying oxygen to enzymes in fibroblasts. To shed light on the functioning of such versatile machinery, we have studied the processes supporting transport of gaseous heme ligands in Cygb. Carbon monoxide rebinding shows a complex kinetic pattern with several distinct reaction intermediates, reflecting rebinding from temporary docking sites, second order recombination, and formation (and dissociation) of a bis-histidyl heme hexacoordinated reaction intermediate…

Genetics and Molecular Biology (all)ProteomicsProtein FoldingProtein ConformationMolecular biologylcsh:MedicineCrystallography X-RayLigandsBiophysics SimulationsBiochemistrychemistry.chemical_compoundProtein structureMacromolecular Structure AnalysisCinètica enzimàticaBinding Sites; Carbon Monoxide; Crystallography X-Ray; Globins; Humans; Kinetics; Ligands; Molecular Dynamics Simulation; Oxygenases; Point Mutation; Protein Binding; Protein Conformation; Medicine (all); Biochemistry Genetics and Molecular Biology (all); Agricultural and Biological Sciences (all)Biomacromolecule-Ligand Interactionslcsh:ScienceHemeCarbon MonoxideCrystallographyHemoproteinsMultidisciplinaryMedicine (all)PhysicsCytoglobinMetabolismeGlobinsBiochemistryOxygenasesddc:500Engineering sciences. TechnologyProtein BindingResearch ArticleBioquímicaProtein StructureBiophysicsReaction intermediateMolecular Dynamics SimulationProtein ChemistryGeneticsHumansPoint MutationGlobinProtein InteractionsBiologyBiologia molecularBinding SitesLigandCytoglobinlcsh:REnzyme kineticsOxygen transportProteinsComputational BiologyKineticsMetabolismAgricultural and Biological Sciences (all)chemistryX-RayBiophysicslcsh:QHuman medicineGenèticaCarbon monoxide
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Acetylcholine-binding protein in the hemolymph of the planorbid snail Biomphalaria glabrata is a pentagonal dodecahedron (60 subunits).

2012

Nicotinic acetylcholine receptors (nAChR) play important neurophysiological roles and are of considerable medical relevance. They have been studied extensively, greatly facilitated by the gastropod acetylcholine-binding proteins (AChBP) which represent soluble structural and functional homologues of the ligand-binding domain of nAChR. All these proteins are ring-like pentamers. Here we report that AChBP exists in the hemolymph of the planorbid snail Biomphalaria glabrata (vector of the schistosomiasis parasite) as a regular pentagonal dodecahedron, 22 nm in diameter (12 pentamers, 60 active sites). We sequenced and recombinantly expressed two ∼25 kDa polypeptides (BgAChBP1 and BgAChBP2) wit…

Macromolecular AssembliesProtein StructureProtein FoldingScienceBiophysicsBiochemistryProtein ChemistryHomology (biology)Ion ChannelsProtein Structure Secondarylaw.inventionDodecahedronAcetylcholine bindinglawHemolymphHemolymphMacromolecular Structure AnalysisBiomphalaria glabrataAnimal PhysiologyAnimalsBiomacromolecule-Ligand InteractionsBiologyAcetylcholine receptorMultidisciplinaryHemoproteinsbiologyBiomphalariaQRActive siteProteinsComputational BiologyAnatomybiology.organism_classificationRecombinant ProteinsAcetylcholineProtein Structure TertiaryBiochemistryAcetylcholine Receptorsbiology.proteinRecombinant DNAMedicineCarrier ProteinsZoologyResearch ArticlePLoS ONE
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Construction of Chimeric Dual-Chain Avidin by Tandem Fusion of the Related Avidins

2011

BackgroundAvidin is a chicken egg-white protein with high affinity to vitamin H, also known as D-biotin. Many applications in life science research are based on this strong interaction. Avidin is a homotetrameric protein, which promotes its modification to symmetrical entities. Dual-chain avidin, a genetically engineered avidin form, has two circularly permuted chicken avidin monomers that are tandem-fused into one polypeptide chain. This form of avidin enables independent modification of the two domains, including the two biotin-binding pockets; however, decreased yields in protein production, compared to wt avidin, and complicated genetic manipulation of two highly similar DNA sequences i…

Macromolecular Assemblieslcsh:MedicineBiosensing TechniquesPolymerase Chain ReactionBiochemistryProtein Structure Secondarychemistry.chemical_compoundProtein structureBiotinMacromolecular Structure AnalysisProtein biosynthesisBiomacromolecule-Ligand InteractionsSurface plasmon resonancelcsh:Science0303 health sciencesMultidisciplinarybiologyrespiratory systemRecombinant ProteinsBiochemistryBiotinylationChromatography GelBiophysic Al SimulationsResearch ArticleProtein StructureStructural similarityRecombinant Fusion Proteins030303 biophysicsBiophysicsBiotinMolecular Dynamics SimulationBiokemia solu- ja molekyylibiologia - Biochemistry cell and molecular biology03 medical and health sciencesstomatognathic systemDefense ProteinsEscherichia coliAnimalsGene familyProtein InteractionsBiology030304 developmental biologylcsh:RProteinsComputational BiologySurface Plasmon ResonanceAvidinchemistrySmall MoleculesFermentationbiology.proteinlcsh:QChickensAvidinPLoS ONE
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Distant Homology Modeling of LCAT and Its Validation through In Silico Targeting and In Vitro and In Vivo Assays

2013

LCAT (lecithin:cholesterol acyltransferase) catalyzes the transacylation of a fatty acid of lecithin to cholesterol, generating a cholesteryl ester and lysolecithin. The knowledge of LCAT atomic structure and the identification of the amino acids relevant in controlling its structure and function are expected to be very helpful to understand the enzyme catalytic mechanism, as involved in HDL cholesterol metabolism. However - after an early report in the late '90 s - no recent advance has been made about LCAT three-dimensional structure. In this paper, we propose an LCAT atomistic model, built following the most up-to-date molecular modeling approaches, and exploiting newly solved crystallog…

MaleModels MolecularProtein StructureDrug Research and DevelopmentProtein Conformationlcsh:MedicineBiologyBiochemistryCatalysisSubstrate SpecificityPhosphatidylcholine-Sterol O-AcyltransferaseMicechemistry.chemical_compoundEnzyme activatorTransacylationProtein structureDrug DiscoveryHydrolaseCatalytic triadBiochemical SimulationsMedicine and Health SciencesAnimalsHumansHomology modelingBiomacromolecule-Ligand Interactionslcsh:SciencePharmacologyBinding SitesPlasma ProteinsMultidisciplinarylcsh:RBiology and Life SciencesProteinsEnzyme structureEnzyme ActivationMolecular Docking SimulationchemistryBiochemistryMutationEnzyme StructureEnzymologyBiocatalysisCholesteryl esterlcsh:QResearch ArticleBiotechnologyPLoS ONE
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Conformational changes in acetylcholine binding protein investigated by temperature accelerated molecular dynamics.

2014

Despite the large number of studies available on nicotinic acetylcholine receptors, a complete account of the mechanistic aspects of their gating transition in response to ligand binding still remains elusive. As a first step toward dissecting the transition mechanism by accelerated sampling techniques, we study the ligand-induced conformational changes of the acetylcholine binding protein (AChBP), a widely accepted model for the full receptor extracellular domain. Using unbiased Molecular Dynamics (MD) and Temperature Accelerated Molecular Dynamics (TAMD) simulations we investigate the AChBP transition between the apo and the agonist-bound state. In long standard MD simulations, both confo…

Nicotinic Acetylcholine ReceptorsProtein ConformationGatingMolecular DynamicsLigandsBiochemistryBiophysics SimulationsIon ChannelsMolecular dynamicsAcetylcholine bindingComputational ChemistryBiochemical SimulationsNicotinic AgonistsBiomacromolecule-Ligand InteractionsBiochemistry SimulationsMultidisciplinaryHydrogen bondChemistryPhysicsQTemperatureRLigand (biochemistry)nicotinic receptor molecular dynamics tamd acethylcholine binding proteinChemistryNicotinic agonistBiochemistryMedicineBiophysic Al SimulationsResearch ArticleProtein BindingProtein subunitScienceBiophysicsMolecular Dynamics SimulationProtein ChemistryStatistical MechanicsChemical BiologyAnimalsBiologyAcetylcholine receptorBinding SitesProteinsComputational BiologyHydrogen BondingSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Protein SubunitsMolluscaAcetylcholine ReceptorsBiophysicsLobelineCarrier ProteinsPLoS ONE
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The hedgehog receptor patched is involved in cholesterol transport.

2011

International audience; BACKGROUND: Sonic hedgehog (Shh) signaling plays a crucial role in growth and patterning during embryonic development, and also in stem cell maintenance and tissue regeneration in adults. Aberrant Shh pathway activation is involved in the development of many tumors, and one of the most affected Shh signaling steps found in these tumors is the regulation of the signaling receptor Smoothened by the Shh receptor Patched. In the present work, we investigated Patched activity and the mechanism by which Patched inhibits Smoothened. METHODOLOGY/PRINCIPAL FINDINGS: Using the well-known Shh-responding cell line of mouse fibroblasts NIH 3T3, we first observed that enhancement …

ciliumlcsh:MedicineyeastBiochemistryReceptors G-Protein-CoupledTransmembrane Transport ProteinsMicechemistry.chemical_compound0302 clinical medicineMolecular Cell Biology[SDV.IDA]Life Sciences [q-bio]/Food engineeringMembrane Receptor SignalingBiomacromolecule-Ligand InteractionsSonic hedgehoglcsh:ScienceComputingMilieux_MISCELLANEOUS0303 health sciencesMultidisciplinaryMechanisms of Signal TransductionVeratrum Alkaloids[SDV.IDA] Life Sciences [q-bio]/Food engineeringdrosophilaSmoothened ReceptorLipidsHedgehog signaling pathwayCell biologySterolsSmoothened ReceptorAlimentation et Nutritionembryonic structurescilMembranes and Sorting[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]Signal transductionvesicular traffickingSignal TransductionResearch Articleprimary ciliumPatched ReceptorsPatchedsignal-transductionanimal structuresCyclopamine[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process EngineeringBiophysicsReceptors Cell Surfacepathway activationSaccharomyces cerevisiaetransduction du signalBiology03 medical and health sciencessonic hedgehoglipidAnimalsHumansFood and NutritionHedgehog Proteins[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringBiology030304 developmental biologyPatched Receptorsprotein signalsCell Membranelcsh:RProteinscholesterolBiological TransportTransmembrane Proteinssterol-sensing domainchemistry[ SDV.NEU ] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]NIH 3T3 Cellscholesterol;lipid;cell trafficking; yeast;drosophila;cells ; pathway activation; vesicular trafficking; signal-transduction; sonic hedgehog;sterol-sensing domain; primary cilium;protein signalsbiology.proteincellslcsh:Qcell traffickingSmoothened030217 neurology & neurosurgery
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