Search results for "allosteric regulation"

showing 10 items of 90 documents

Selectivity of pharmacological tools: implications for use in cell physiology. A Review in the Theme: Cell Signaling: Proteins, Pathways and Mechanis…

2014

Pharmacological inhibitors are frequently used to identify the receptors, receptor subtypes, and associated signaling pathways involved in physiological cell responses. Based on the effects of such inhibitors conclusions are drawn about the involvement of their assumed target or lack thereof. While such inhibitors can be useful tools for a better physiological understanding, their uncritical use can lead to incorrect conclusions. This article reviews the concept of inhibitor selectivity and its implication for cell physiology. Specifically, we discuss the implications of using inhibitor vs. activator approaches, issues of direct vs. indirect pathway modulation, implications of inverse agoni…

Cell physiologyCell signalingPhysiologyAdrenergic beta-AntagonistsCellAllosteric regulationImidazolesCell CommunicationCell BiologyAdrenergic beta-AgonistsBiologyPharmacologyIndirect pathway of movementCell Physiological PhenomenaReceptors G-Protein-CoupledFunctional antagonismmedicine.anatomical_structuremedicineAnimalsHumansSignal transductionReceptorNeuroscienceProtein BindingSignal TransductionAmerican Journal of Physiology-Cell Physiology
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Synthesis, characterization and X-ray crystal structures of cyclam derivatives. 7. Hydrogen-bond induced allosteric effects and protonation cooperati…

2005

The unprecedented cooperative protonation properties displayed by a barrel-shaped macrotricyclic tetraamine incorporating two 14-membered bisamide rings maintained in a face-to-face arrangement is rationalized in terms of allosteric effects upon binding of the first and third protons.

ChemistryHydrogen bondStereochemistryAllosteric regulationX-rayCooperativityProtonationGeneral ChemistryCrystal structureCatalysisCharacterization (materials science)chemistry.chemical_compoundCyclamMaterials ChemistryNew Journal of Chemistry
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Allosteric modulation of nicotinic acetylcholine receptors as a treatment strategy for Alzheimer's disease

2000

The basic symptoms of Alzheimer's dementia, i.e., a loss in cognitive function, are due to impaired nicotinic cholinergic neurotransmission. To compensate for this impairment by drug treatment, blockers of the acetylcholine-degrading enzyme acetylcholinesterase are applied, even though this approach obviously is prone to many side-effects, including those of muscarinic nature. We have recently described a novel class of nicotinic acetylcholine receptor ligands which, similar to the action of benzodiazepines on GABA(A) receptors, allosterically potentiate submaximal nicotinic responses. The sensitizing effect is a consequence of facilitated channel opening in the presence of allosterically p…

Cholinergic AgentsReceptors NicotinicNeurotransmissionPharmacologyPC12 Cellschemistry.chemical_compoundCognitionAllosteric RegulationAlzheimer DiseaseMuscarinic acetylcholine receptormedicineAnimalsHumansLearningCells CulturedAcetylcholine receptorPharmacologyNeurotransmitter AgentsGalantamineAcetylcholinesteraseRatsNicotinic acetylcholine receptorNicotinic agonistchemistryCholinesterase InhibitorsAlpha-4 beta-2 nicotinic receptorNeuroscienceAcetylcholinemedicine.drugEuropean Journal of Pharmacology
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Control of kinetics by cooperative interactions.

2011

Cooperative effects in ligand binding and dissociation kinetics are much less investigated than steady state kinetics or equilibrium binding. Nevertheless, cooperativity in ligand binding leads necessarily to characteristic properties with respect to kinetic properties of the system. In case of positive cooperativity as found in oxygen binding proteins, a typical property is an autocatalytic ligand dissociation behavior leading to a time dependent, apparent ligand dissociation rate. To follow systematically the influence of the various potentially involved parameters on this characteristic property, simulations based on the simple MWC model were performed which should be relevant for all ty…

Clinical BiochemistryAllosteric regulationCooperative bindingThermodynamicsProteinsCooperativityCell BiologyLigand (biochemistry)LigandsBiochemistryDissociation (chemistry)Crystallographychemistry.chemical_compoundKineticschemistryAllosteric RegulationModels ChemicalGeneticsCharacteristic propertyMolecular BiologyOxygen bindingEquilibrium constantProtein BindingIUBMB life
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Dynamic-shared Pharmacophore Approach as Tool to Design New Allosteric PRC2 Inhibitors, Targeting EED Binding Pocket.

2020

Abstract: The Polycomb Repressive complex 2 (PRC2) maintains a repressive chromatin state and silences many genes, acting as methylase on histone tails. This enzyme was found overexpressed in many types of cancer. In this work, we have set up a Computer-Aided Drug Design approach based on the allosteric modulation of PRC2. In order to minimize the possible bias derived from using a single set of coordinates within the protein-ligand complex, a dynamic workflow was developed. In details, molecular dynamic was used as tool to identify the most significant ligand-protein interactions from several crystallized protein structures. The identified features were used for the creation of dynamic pha…

Computer scienceAllosteric regulationBinding pocketmacromolecular substancesComputational biologyMolecular Dynamics SimulationLigands01 natural sciences03 medical and health sciencesProtein structureStructural BiologyDrug DiscoveryHumans030304 developmental biologyEED0303 health sciencesVirtual screeningBinding SitesbiologyOrganic ChemistryMolecular DynamicPolycomb Repressive Complex 2Dynamic pharmacophorePRC20104 chemical sciencesComputer Science ApplicationsChromatinMolecular Docking Simulation010404 medicinal & biomolecular chemistryROC CurveDocking (molecular)Drug Designbiology.proteinMolecular MedicinePharmacophorePRC2Allosteric SiteProtein BindingMolecular informaticsReferences
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A conformationally adaptive macrocycle : conformational complexity and host–guest chemistry of zorb[4]arene

2018

Large amplitude conformational change is one of the features of biomolecular recognition and is also the basis for allosteric effects and signal transduction in functional biological systems. However, synthetic receptors with controllable conformational changes are rare. In this article, we present a thorough study on the host–guest chemistry of a conformationally adaptive macrocycle, namely per-O-ethoxyzorb[4]arene (ZB4). Similar to per-O-ethoxyoxatub[4]arene, ZB4 is capable of accommodating a wide range of organic cations. However, ZB4 does not show large amplitude conformational responses to the electronic substituents on the guests. Instead of a linear free-energy relationship, ZB4 foll…

Conformational changeAllosteric regulationSupramolecular chemistryCrystal structure010402 general chemistry01 natural sciencesHeat capacityFull Research Papersupramolecular chemistrylcsh:QD241-441lcsh:Organic chemistryComputational chemistrysupramolekulaarinen kemiahost-guest chemistryhost–guest chemistrylcsh:ScienceHost–guest chemistryta116010405 organic chemistryChemistryComponent (thermodynamics)Hydrogen bondOrganic Chemistryzorb[4]arene0104 chemical sciencesChemistrymacrocyclesconformationslcsh:QBeilstein Journal of Organic Chemistry
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The Study of Carbamoyl Phosphate Synthetase 1 Deficiency Sheds Light on the Mechanism for Switching On/Off the Urea Cycle

2015

12 páginas, 4 figuras, 2 tablas.

Conformational changeCarbamoyl-Phosphate Synthase I Deficiency DiseaseAllosteric regulationCarbamoyl-Phosphate Synthase (Ammonia)Urea cycle diseases610 Medicine & healthBiologyMolecular Dynamics Simulationurologic and male genital diseases03 medical and health sciences0302 clinical medicineGlutamates1311 GeneticsAmmoniaEnzyme StabilityGeneticsmedicine1312 Molecular BiologyHumansUreaHyperammonemiaSite-directed mutagenesisMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesSite-directed mutagenesisurogenital systemMutagenesisCarbamoyl phosphate synthetase 1HyperammonemiaCarbamoyl phosphate synthetasemedicine.diseaseAllosteric regulation3. Good healthProtein Structure TertiaryRestrained molecular dynamicsKineticsEnzymeBiochemistrychemistry10036 Medical ClinicEnzymeUrea cycleMutationInborn errors030217 neurology & neurosurgerySignal Transduction
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Decipher the mechanisms of protein conformational changes induced by nucleotide binding through free-energy landscape analysis: ATP binding to Hsp70.

2013

ATP regulates the function of many proteins in the cell by transducing its binding and hydrolysis energies into protein conformational changes by mechanisms which are challenging to identify at the atomic scale. Based on molecular dynamics (MD) simulations, a method is proposed to analyze the structural changes induced by ATP binding to a protein by computing the effective free-energy landscape (FEL) of a subset of its coordinates along its amino-acid sequence. The method is applied to characterize the mechanism by which the binding of ATP to the nucleotide-binding domain (NBD) of Hsp70 propagates a signal to its substrate-binding domain (SBD). Unbiased MD simulations were performed for Hsp…

Conformational changeProtein ConformationAllosteric regulationPlasma protein bindingMolecular Dynamics SimulationCellular and Molecular NeuroscienceProtein structureAdenosine TriphosphateGeneticsHSP70 Heat-Shock ProteinsMolecular Biologylcsh:QH301-705.5Nuclear Magnetic Resonance BiomolecularEcology Evolution Behavior and SystematicsEcologybiologyChemistryEscherichia coli ProteinsEnergy landscapeComputational Theory and MathematicsBiochemistrylcsh:Biology (General)Docking (molecular)Modeling and SimulationChaperone (protein)Biophysicsbiology.proteinBinding domainProtein BindingResearch ArticlePLoS computational biology
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The Allosteric Effector l-Lactate Induces a Conformational Change of 2×6-meric Lobster Hemocyanin in the Oxy State as Revealed by Small Angle X-ray S…

2001

Abstract Hemocyanins are multisubunit respiratory proteins found in many invertebrates. They bind oxygen highly cooperatively. However, not much is known about the structural basis of this behavior. We studied the influence of the physiological allosteric effectorl-lactate on the oxygenated quaternary structure of the 2×6-meric hemocyanin from the lobster Homarus americanus employing small angle x-ray scattering (SAXS). The presence of 20 mm l-lactate resulted in different scattering curves compared with those obtained in the absence of l-lactate. The distance distribution functionsp(r) indicated a more compact molecule in presence ofl-lactate, which is also reflected in a reduction of the …

Conformational changeProtein ConformationScatteringChemistrySmall-angle X-ray scatteringmedicine.medical_treatmentAllosteric regulationHemocyaninCell BiologyBiochemistryNephropidaeMicroscopy ElectronCrystallographyAllosteric RegulationHemocyaninsRadius of gyrationmedicineAnimalsScattering RadiationProtein quaternary structureLactic AcidMolecular BiologyOxygen bindingJournal of Biological Chemistry
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Human Inducible Hsp70: Structures, Dynamics, and Interdomain Communication from All-Atom Molecular Dynamics Simulations

2015

The 70 kDa human heat shock protein is a major molecular chaperone involved in de novo folding of proteins in vivo and refolding of proteins under stress conditions. Hsp70 is related to several "misfolding diseases" and other major pathologies, such as cancer, and is a target for new therapies. Hsp70 is comprised of two main domains: an N-terminal nucleotide binding domain (NBD) and a C-terminal substrate protein binding domain (SBD). The chaperone function of Hsp70 is based on an allosteric mechanism. Binding of ATP in NBD decreases the affinity of the substrate for SBD, and hydrolysis of ATP is promoted by binding of polypeptide segments in the SBD. No complete structure of human Hsp70 is…

Conformational changebiologySaccharomyces cerevisiaeAllosteric regulationPlasma protein bindingbiology.organism_classificationComputer Science ApplicationsMolecular dynamicsBiochemistryCyclic nucleotide-binding domainATP hydrolysisChaperone (protein)biology.proteinBiophysicsPhysical and Theoretical ChemistryJournal of Chemical Theory and Computation
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