Search results for "allostery"

showing 5 items of 5 documents

Recent advances in computational design of potent aromatase inhibitors: open-eye on endocrine-resistant breast cancers.

2019

Introduction: The vast majority of breast cancers (BC) are estrogen receptor positive (ER+). The most effective treatments to fight this BC type rely on estrogen deprivation therapy, by inhibiting the aromatase enzyme, which performs estrogen biosynthesis, or on blocking the estrogens signaling path via modulating/degrading the estrogen's specific nuclear receptor (estrogen receptor-?, ER?). While being effective at early disease stage, patients treated with aromatase inhibitors (AIs) may acquire resistance and often relapse after prolonged therapies. Areas covered: In this compendium, after an overview of the historical development of the AIs currently in clinical use, and of the computati…

Antineoplastic Agents Hormonalmedicine.drug_classCYP450sEstrogen receptorallostery; aromatase inhibitors; Breast cancer; CYP450s; ligand-based and structure-based drug design; molecular dynamics; virtual screeningBreast NeoplasmsMolecular Dynamics SimulationBioinformatics03 medical and health sciencesBreast cancer0302 clinical medicineBreast cancerDrug DiscoverymedicineEndocrine systemHumansAromataseSurvival rate030304 developmental biologyCause of deathNeoplasm Staging0303 health sciencesallosterybiologybusiness.industryAromatase Inhibitorsvirtual screeningmedicine.diseaseligand-based and structure-based drug designmolecular dynamicsSurvival RateNuclear receptorEstrogenDrug Resistance Neoplasm030220 oncology & carcinogenesisDrug Designbiology.proteinFemalebusinessExpert opinion on drug discovery
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A lipid transfer protein binds to a receptor involved in the control of plant defence responses

2001

AbstractLipid transfer proteins (LTPs) and elicitins are both able to load and transfer lipidic molecules and share some structural and functional properties. While elicitins are known as elicitors of plant defence mechanisms, the biological function of LTP is still an enigma. We show that a wheat LTP1 binds with high affinity sites. Binding and in vivo competition experiments point out that these binding sites are common to LTP1 and elicitins and confirm that they are the biological receptors of elicitins. A mathematical analysis suggests that these receptors could be represented by an allosteric model corresponding to an oligomeric structure with four identical subunits.

Models Molecular0106 biological sciencesTime FactorsProtein ConformationPlasma protein bindingLigands01 natural sciencesBiochemistryProtein structureStructural BiologyReceptorAllosteryTriticumComputingMilieux_MISCELLANEOUSPlant Proteins0303 health sciencesFungal proteinfood and beveragesCell biologyBiochemistryPlant lipid transfer proteinsAllosteric SiteProtein BindingReceptorPhytophthoraLipid transfer proteinAllosteric regulationBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyBinding CompetitiveFungal Proteins03 medical and health sciencesTobaccoGeneticsBinding site[SDV.BC] Life Sciences [q-bio]/Cellular BiologyMolecular Biology030304 developmental biologyBinding SitesDose-Response Relationship DrugAlgal ProteinsCell MembraneElicitinCell BiologyAntigens PlantModels TheoreticalLipid MetabolismElicitinCarrier Proteins010606 plant biology & botanyFEBS Letters
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The Monod-Wyman-Changeux allosteric model accounts for the quaternary transition dynamics in wild type and a recombinant mutant human hemoglobin

2012

International audience; The acknowledged success of the Monod-Wyman-Changeux (MWC) allosteric model stems from its efficacy in accounting for the functional behavior of many complex proteins starting with hemoglobin (the paradigmatic case) and extending to channels and receptors. The kinetic aspects of the allosteric model, however, have been often neglected, with the exception of hemoglobin and a few other proteins where conformational relaxations can be triggered by a short and intense laser pulse, and monitored by time-resolved optical spectroscopy. Only recently the application of time-resolved wide-angle X-ray scattering (TR-WAXS), a direct structurally sensitive technique, unveiled th…

Models MolecularProtein ConformationcooperativityMESH: Catalytic DomainCooperativity01 natural sciencesMESH: Recombinant ProteinsHemoglobinsProtein structureMESH: Protein ConformationCatalytic Domainprotein structural dynamicsMESH: Allosteric Site0303 health sciencesMultidisciplinaryallosterybiologyMESH: KineticsChemistryBiological SciencesRecombinant Proteins[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsMESH: HemoglobinsAllosteric SiteMESH: Models MolecularAdultMESH: MutationStereochemistryKineticsAllosteric regulation010402 general chemistry03 medical and health sciencesprotein conformational changesflash photolysisallostery; cooperativity; flash photolysis; hemoglobin; protein conformational changes; protein structural dynamics; time-resolved wide angle x ray scattering; time-resolved x-ray scatteringHumans030304 developmental biologytime-resolved X-ray scattering; protein conformational changes; cooperativity; flash photolysisMESH: Humanstime-resolved X-ray scatteringWild typeActive sitetime-resolved wide angle x ray scatteringMESH: AdulthemoglobinSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)0104 chemical sciencesprotein conformational changeKineticsAllosteric enzymeMutationbiology.proteinHemoglobin
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Unveiling the timescale of the R-T transition in human hemoglobin.

2010

Time-resolved wide-angle X-ray scattering, a recently developed technique allowing to probe global structural changes of proteins in solution, was used to investigate the kinetics of R-T quaternary transition in human hemoglobin and to systematically compare it to that obtained with time-resolved optical spectroscopy under nearly identical experimental conditions. Our data reveal that the main structural rearrangement associated with the R-T transition takes place approximately 2 mus after the photolysis of hemoglobin at room temperature and neutral pH. This finding suggests that the 20-mus step observed with time-resolved optical spectroscopy corresponds to a small and localized structural…

PhotochemistryProtein ConformationKineticsMethemoglobinHemoglobinsStructural BiologyHumansScattering RadiationSpectroscopyMolecular BiologyallosteryScatteringChemistryProtein dynamicsSpectrum AnalysisPhotodissociationhemoglobinHydrogen-Ion ConcentrationSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)CrystallographyKineticsStructural changeChemical physicshemoglobin; allostery; protein dynamicsprotein dynamicssense organsHemoglobinJournal of molecular biology
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The Interconnecting Hairpin Extension "Arm": An Essential Allosteric Element of Phytochrome Activity

2023

In red-light sensing phytochromes, isomerization of the bilin chromophore triggers structural and dynamic changes across multiple domains, ultimately leading to control of the output module (OPM) activity. In between, a hairpin structure, "arm", extends from an interconnecting domain to the chromophore region. Here, by removing this protein segment in a bacteriophytochrome from Deinococcus radiodurans (DrBphP), we show that the arm is crucial for signal transduction. Crystallographic, spectroscopic, and biochemical data indicate that this variant maintains the properties of DrBphP in the resting state. Spectroscopic data also reveal that the armless systems maintain the ability to respond t…

phytochromesoluviestintäphotosensorallostery92-11histidine kinanasephotoreceptorthermal stabilityreseptorit (biokemia)87.1592-05structure and functionproteiinitvalokemia87.14 2000 MSCprotein structurePACSsignal transduction
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