Search results for "binding"

showing 10 items of 3896 documents

The C-terminal region of human plasma fetuin-B is dispensable for the raised-elephant-trunk mechanism of inhibition of astacin metallopeptidases

2019

© The Author(s) 2019.

0301 basic medicineProteasesProtein Conformationlcsh:MedicineAstacoideaCrystallography X-RayCleavage (embryo)Protein Structure SecondaryArticleMice03 medical and health sciencesScissile bondHydrolaseAnimalsHumansAmino Acid Sequencelcsh:ScienceProtein secondary structureX-ray crystallographyBinding SitesMultidisciplinary030102 biochemistry & molecular biologyChemistrylcsh:RMetalloendopeptidasesProteasesFetuinFetuin-BCell biologyZincFertility030104 developmental biologyProteolysisMetalloproteaseslcsh:QAstacinLinkerScientific Reports
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Discovery and validation of 2-styryl substituted benzoxazin-4-ones as a novel scaffold for rhomboid protease inhibitors

2017

Abstract Rhomboids are intramembrane serine proteases with diverse physiological functions in organisms ranging from archaea to humans. Crystal structure analysis has provided a detailed understanding of the catalytic mechanism, and rhomboids have been implicated in various disease contexts. Unfortunately, the design of specific rhomboid inhibitors has lagged behind, and previously described small molecule inhibitors displayed insufficient potency and/or selectivity. Using a computer-aided approach, we focused on the discovery of novel scaffolds with reduced liabilities and the possibility for broad structural variations. Docking studies with the E. coli rhomboid GlpG indicated that 2-styry…

0301 basic medicineProteasesSerine Proteinase InhibitorsStereochemistrymedicine.medical_treatmentClinical BiochemistryPharmaceutical ScienceBiochemistryStyrenesSerine03 medical and health sciencesCatalytic DomainEndopeptidasesDrug DiscoveryEscherichia coliSerinemedicineAnimalsChymotrypsinDrosophila ProteinsHumansMolecular BiologyEnzyme AssaysSerine proteaseProtease030102 biochemistry & molecular biologybiologyBenzoxazinonesChemistryEscherichia coli ProteinsRhomboid proteaseRhomboidOrganic ChemistryMembrane ProteinsTransforming Growth Factor alphaBenzoxazinesDNA-Binding ProteinsMolecular Docking Simulation030104 developmental biologyDocking (molecular)Mutationbiology.proteinMolecular MedicineCattleDrosophilaBioorganic & Medicinal Chemistry Letters
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Searching for Chymase Inhibitors among Chamomile Compounds Using a Computational-Based Approach

2018

Inhibitors of chymase have good potential to provide a novel therapeutic approach for the treatment of cardiovascular diseases. We used a computational approach based on pharmacophore modeling, docking, and molecular dynamics simulations to evaluate the potential ability of 13 natural compounds from chamomile extracts to bind chymase enzyme. The results indicated that some chamomile compounds can bind to the active site of human chymase. In particular, chlorogenic acid had a predicted binding energy comparable or even better than that of some known chymase inhibitors, interacted stably with key amino acids in the chymase active site, and appeared to be more selective for chymase than other …

0301 basic medicineProteaseschlorogenic acidlcsh:QR1-502030204 cardiovascular system & hematologyMolecular Dynamics SimulationCrystallography X-RayLigandsBiochemistrylcsh:MicrobiologyArticleSerine03 medical and health sciences0302 clinical medicineChymasesCatalytic DomainHumanschamomilecardiovascular diseases; chamomile; chlorogenic acid; chymase; docking; matricin; molecular dynamics simulations; pharmacophore; Biochemistry; Molecular BiologyEnzyme InhibitorsMolecular Biologychymasechemistry.chemical_classificationBinding SitesbiologypharmacophoreChymaseActive sitemolecular dynamics simulationsmatricinAmino acidcardiovascular diseasesMolecular Docking Simulation030104 developmental biologyEnzymechemistryBiochemistryDocking (molecular)dockingbiology.proteinPharmacophoreBiomolecules
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Phosphorylation and proteasome recognition of the mRNA- binding protein Cth2 facilitates yeast adaptation to iron deficiency

2018

Iron is an indispensable micronutrient for all eukaryotic organisms due to its participation as a redox cofactor in many metabolic pathways. Iron imbalance leads to the most frequent human nutritional deficiency in the world. Adaptation to iron limitation requires a global reorganization of the cellular metabolism directed to prioritize iron utilization for essential processes. In response to iron scarcity, the conserved Saccharomyces cerevisiae mRNA-binding protein Cth2, which belongs to the tristetraprolin family of tandem zinc finger proteins, coordinates a global remodeling of the cellular metabolism by promoting the degradation of multiple mRNAs encoding highly iron-consuming proteins.…

0301 basic medicineProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsIronPosttranslational regulationSaccharomyces cerevisiaeMrna bindingMicrobiology03 medical and health sciencesProtein stabilityTristetraprolinGene Expression Regulation FungalVirologyPolitical scienceProtein stabilitySerineRNA MessengerPhosphorylationIron deficiencyAdaptation PhysiologicalQR1-502Yeast030104 developmental biologyMutagenesisChristian ministryProtein Processing Post-TranslationalHumanities
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Permeating disciplines: Overcoming barriers between molecular simulations and classical structure-function approaches in biological ion transport

2017

Ion translocation across biological barriers is a fundamental requirement for life. In many cases, controlling this process-for example with neuroactive drugs-demands an understanding of rapid and reversible structural changes in membrane-embedded proteins, including ion channels and transporters. Classical approaches to electrophysiology and structural biology have provided valuable insights into several such proteins over macroscopic, often discontinuous scales of space and time. Integrating these observations into meaningful mechanistic models now relies increasingly on computational methods, particularly molecular dynamics simulations, while surfacing important challenges in data manage…

0301 basic medicineProtein ConformationComputer sciencemedia_common.quotation_subjectData managementBiophysicsContext (language use)Molecular Dynamics SimulationBiochemistryIon ChannelsArticleStructure-Activity Relationship03 medical and health sciencesAnimalsHumansFunction (engineering)Biological sciencesClassical structureIon transportermedia_commonIon Transportbusiness.industryMembrane Transport ProteinsCell BiologyData science030104 developmental biologyStructural biologybusinessIon Channel GatingProtein BindingBiochimica et Biophysica Acta (BBA) - Biomembranes
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Direct Visualization of the Conformational Dynamics of Single Influenza Hemagglutinin Trimers

2018

Influenza hemagglutinin (HA) is the canonical type I viral envelope glycoprotein and provides a template for the membrane-fusion mechanisms of numerous viruses. The current model of HA-mediated membrane fusion describes a static "spring-loaded" fusion domain (HA2) at neutral pH. Acidic pH triggers a singular irreversible conformational rearrangement in HA2 that fuses viral and cellular membranes. Here, using single-molecule Förster resonance energy transfer (smFRET)-imaging, we directly visualized pH-triggered conformational changes of HA trimers on the viral surface. Our analyses reveal reversible exchange between the pre-fusion and two intermediate conformations of HA2. Acidification of p…

0301 basic medicineProtein ConformationHemagglutinin (influenza)Hemagglutinin Glycoproteins Influenza VirusBiologyArticleGeneral Biochemistry Genetics and Molecular BiologyReaction coordinate03 medical and health sciencesViral envelopeInfluenza HumanFluorescence Resonance Energy TransferHumansDynamic equilibriumFusionCell MembraneLipid bilayer fusionHydrogen-Ion ConcentrationVirus InternalizationSingle Molecule ImagingHEK293 CellsHemagglutinins030104 developmental biologyMembraneFörster resonance energy transferA549 CellsInfluenza A virusBiophysicsbiology.proteinProtein BindingCell
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The Crystal Structure of Gurmarin, a Sweet Taste–Suppressing Protein: Identification of the Amino Acid Residues Essential for Inhibition

2018

International audience; Gurmarin is a highly specific sweet-taste suppressing protein in rodents that is isolated from the Indian plant Gymnemasylvestre. Gurmarin consists of 35 amino acid residues containing three intramolecular disulfide bridges that form a cystine knot. Here, we report the crystal structure of gurmarin at a 1.45 Å resolution and compare it with previously reported NMR solution structures. The atomic structure at this resolution allowed us to identify a very flexible region consisting of hydrophobic residues. Some of these amino acid residues had been identified as a putative binding site for the rat sweet taste receptor in a previous study. By combining alanine-scanning …

0301 basic medicineProtein ConformationPhysiologyCrystal structureCrystallography X-Ray03 medical and health sciencesBehavioral NeuroscienceGPCRsweet tastetaste receptorPhysiology (medical)goût sucréAnimalsHumansG protein-coupled receptorAmino AcidsBinding siteReceptorNuclear Magnetic Resonance BiomolecularPlant ProteinsGurmarininhibiteur030102 biochemistry & molecular biologybiologyChemistryMutagenesisCystine knotGymnema sylvestreSweet tastebiology.organism_classificationRecombinant ProteinsSensory SystemsRats3. Good healthinhibitorHEK293 Cells030104 developmental biologyBiochemistryGymnema sylvestreknottin[SDV.AEN]Life Sciences [q-bio]/Food and NutritionHydrophobic and Hydrophilic InteractionsChemical Senses
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Evaluating the stability of pharmacophore features using molecular dynamics simulations.

2016

Abstract Molecular dynamics simulations of twelve protein—ligand systems were used to derive a single, structure based pharmacophore model for each system. These merged models combine the information from the initial experimental structure and from all snapshots saved during the simulation. We compared the merged pharmacophore models with the corresponding PDB pharmacophore models, i.e., the static models generated from an experimental structure in the usual manner. The frequency of individual features, of feature types and the occurrence of features not present in the static model derived from the experimental structure were analyzed. We observed both pharmacophore features not visible in …

0301 basic medicineProtein FlexibilityProtein ConformationBiophysicsStability (learning theory)Molecular Dynamics SimulationLigands01 natural sciencesBiochemistryLigandScoutSet (abstract data type)03 medical and health sciencesMolecular dynamicsComputational chemistryFeature (machine learning)Pharmacophore ModelingSensitivity (control systems)Molecular BiologyBinding Sites010405 organic chemistryChemistryStructure-based Pharmacophore ModelingMolecular DynamicProteinsHydrogen BondingCell Biology0104 chemical sciences030104 developmental biologyRankingModels ChemicalDrug DesignPharmacophoreBiological systemProtein BindingBiochemical and biophysical research communications
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Plasmin-Induced Activation of Human Platelets Is Modulated by Thrombospondin-1, Bona Fide Misfolded Proteins and Thiol Isomerases

2020

Inflammatory processes are triggered by the fibrinolytic enzyme plasmin. Tissue-type plasminogen activator, which cleaves plasminogen to plasmin, can be activated by the cross-&beta

0301 basic medicineProtein FoldingPlatelet AggregationPlasmin030204 cardiovascular system & hematologyProtein aggregationFibrinogenThrombospondin 10302 clinical medicinePlateletFibrinolysinprotein misfoldingIsomerasesSpectroscopyChemistryfood and beveragesGeneral Medicinethiol-isomerasesComputer Science ApplicationsCell biologyP-Selectinplateletsmedicine.drugcirculatory and respiratory physiologyBlood PlateletsCatalysisArticleInorganic Chemistry03 medical and health sciencesProtein AggregatesThrombospondin 1medicineHumansPlatelet activationSulfhydryl CompoundsPhysical and Theoretical Chemistrythrombospondin-1Molecular BiologyplasminInflammationOrganic ChemistryfungiFibrinogen bindingFibrinogenPlasminogenPlatelet Activation030104 developmental biologyProtein Conformation beta-StrandPeptidesPlasminogen activatorInternational Journal of Molecular Sciences
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Lack of NFATc1 SUMOylation prevents autoimmunity and alloreactivity

2020

A novel transgenic mouse, in which the transcription factor NFATc1 bears lysine-to-arginine mutations that prevent modification by SUMO, develops normally and is healthy. However, SUMO-insensitive NFATc1 transmits strong tolerogenic signals, thus preventing autoimmune and alloimmune T cell responses.

0301 basic medicineProtein sumoylationEncephalomyelitis Autoimmune ExperimentalT cellStem Cells & RegenerationImmunologySUMO proteinAutoimmunityBiologyenvironment and public healthT-Lymphocytes RegulatoryArticleMinor Histocompatibility AntigensMice03 medical and health sciences0302 clinical medicineImmune systemNeuroinflammationAldesleukinSTAT5 Transcription FactormedicineAnimalsImmunology and AllergyTranscription factorMice Knockoutintegumentary systemNFATC Transcription FactorsExperimental autoimmune encephalomyelitisSumoylationNFATmedicine.diseaseCell biologyenzymes and coenzymes (carbohydrates)030104 developmental biologymedicine.anatomical_structureProto-Oncogene Proteins c-bcl-2030220 oncology & carcinogenesisCytokinesPositive Regulatory Domain I-Binding Factor 1Journal of Experimental Medicine
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