Search results for "binding"

showing 10 items of 3896 documents

Features of TAP-independent MHC class I ligands revealed by quantitative mass spectrometry.

2008

TAP is responsible for transferring cytosolic peptides into the ER, where they can be loaded onto MHC molecules. Deletion of TAP results in a drastic reduction of MHC class I surface expression and alters the presented peptide pattern. This key molecule in antigen processing is tackled by several viruses and lost in some tumors, rendering the altered cells less vulnerable to T cell-based immune surveillance. Using the TAP-deficient cell line LCL721.174 and its TAP-expressing progenitor cell line LCL721.45, we identified and quantified more than 160 HLA ligands, 50 of which were presented TAP-independently. Peptides which were predominantly presented on the TAP-deficient LCL721.174 cell line…

Proteasome Endopeptidase ComplexImmunologyAntigen presentationEpitopes T-LymphocyteGene ExpressionHuman leukocyte antigenCysteine Proteinase InhibitorsProtein Sorting SignalsMajor histocompatibility complexCell LineAntigenATP Binding Cassette Transporter Subfamily B Member 3HLA AntigensTandem Mass SpectrometryMHC class IHLA-A2 AntigenImmunology and AllergyHumansAmino Acid SequenceATP Binding Cassette Transporter Subfamily B Member 2Antigen PresentationbiologyHLA-A AntigensAntigen processingHistocompatibility Antigens Class IProteinsTransporter associated with antigen processingMHC restrictionMolecular biologyPeptide FragmentsCell biologyHLA-B AntigensIsotope Labelingbiology.proteinATP-Binding Cassette TransportersProteasome InhibitorsGene DeletionProtein BindingEuropean journal of immunology
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Development of Novel Selective Peptidomimetics Containing a Boronic Acid Moiety, Targeting the 20S Proteasome as Anticancer Agents

2014

This paper describes the design, synthesis, and biological evaluation of peptidomimetic boronates as inhibitors of the 20S proteasome, a validated target in the treatment of multiple myeloma. The synthesized compounds showed a good inhibitory profile against the ChT-L activity of 20S proteasome. Compounds bearing a β-alanine residue at the P2 position were the most active, that is, 3-ethylphenylamino and 4-methoxyphenylamino (R)-1-{3-[4-(substituted)-2-oxopyridin-1(2H)-yl]propanamido}-3-methylbutylboronic acids (3 c and 3 d, respectively), and these derivatives showed inhibition constants (Ki ) of 17 and 20 nM, respectively. In addition, they co-inhibited post glutamyl peptide hydrolase act…

Proteasome Endopeptidase ComplexPeptidomimeticStereochemistryCell Survivalanticancer agents; boronates; bortemib; Docking studies; Peptidomimetics; inhibitor; proteasomesAntineoplastic AgentsSaccharomyces cerevisiaedocking studieBiochemistrySubstrate Specificitychemistry.chemical_compoundCell Line TumorDrug DiscoverymedicineMoietyHumansGeneral Pharmacology Toxicology and PharmaceuticsPharmacologychemistry.chemical_classificationBinding SitesproteasomesBortezomibOrganic ChemistrybortezomibboronateBoronic AcidspeptidomimeticProtein Structure Tertiaryanticancer agentMolecular Docking SimulationinhibitorEnzymechemistryProteasomeBiochemistryDocking (molecular)Molecular MedicinePeptidomimeticsGrowth inhibitionDrug Screening Assays AntitumorProteasome InhibitorsBoronic acidmedicine.drug
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SUMOylation of Blimp-1 promotes its proteasomal degradation

2011

Abstract B lymphocyte induced maturation protein-1 (Blimp-1) is a transcription repressor of the Krueppel-like family. Blimp-1 plays important roles in developmental processes, such as of germ cells and hair follicle stem cells. In B lymphocytes Blimp-1 orchestrates the terminal differentiation into plasma cells. We discovered that Blimp-1 undergoes SUMOylation by SUMO-1. This SUMOylation is modulated by the SUMO protease SENP1. While Blimp-1 is relatively stable in 293T cells, a fusion with SUMO1 rendered it to rapid proteasomal degradation. Increase in SENP1 activity stabilized Blimp-1, while a decrease promoted its degradation. Our data indicate that SUMOylation of Blimp-1 regulates its …

Proteasome Endopeptidase ComplexSENP1ImmunoprecipitationSUMO-1 ProteinBiophysicsSUMO proteinPlasma cellPlasma cellBiologyBiochemistryCell LineProtein–protein interactionSENP1Structural BiologyEndopeptidasesGeneticsmedicineHumansMolecular BiologyProteasomeProtein StabilityHEK 293 cellsSumoylationCell BiologyCell biologyRepressor ProteinsCysteine Endopeptidasesmedicine.anatomical_structureProteasomeSUMO proteasePositive Regulatory Domain I-Binding Factor 1IntracellularFEBS Letters
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Immunoproteasome and Non-Covalent Inhibition: Exploration by Advanced Molecular Dynamics and Docking Methods

2021

The selective inhibition of immunoproteasome is a valuable strategy to treat autoimmune, inflammatory diseases, and hematologic malignancies. Recently, a new series of amide derivatives as non-covalent inhibitors of the β1i subunit with Ki values in the low/submicromolar ranges have been identified. Here, we investigated the binding mechanism of the most potent and selective inhibitor, N-benzyl-2-(2-oxopyridin-1(2H)-yl)propanamide (1), to elucidate the steps from the ligand entrance into the binding pocket to the ligand-induced conformational changes. We carried out a total of 400 ns of MD-binding analyses, followed by 200 ns of plain MD. The trajectories clustering allowed identifying thre…

Proteasome Endopeptidase ComplexStereochemistryPharmaceutical ScienceOrganic chemistryinduced-fit dockingMolecular Dynamics Simulation01 natural sciencesArticlemetadynamicsAnalytical Chemistry03 medical and health scienceschemistry.chemical_compoundimmunoproteasomeQD241-441AmideDrug DiscoveryOrganosilicon CompoundsPhysical and Theoretical Chemistrynon-covalent inhibitor030304 developmental biology0303 health sciencesBinding Sites010405 organic chemistrymolecular dynamicnon-covalent inhibitorsMetadynamicsRational designDipeptidesLigand (biochemistry)PropanamideSettore CHIM/08 - Chimica Farmaceuticamolecular dynamics0104 chemical sciencesMolecular Docking SimulationchemistryChemistry (miscellaneous)Docking (molecular)MD bindingMolecular MedicinemetadynamicLead compoundOligopeptidesProteasome InhibitorsAcetamideProtein BindingMolecules
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Development and characterization of mouse anti-human LMP2, LMP7, TAP1 and TAP2 monoclonal antibodies.

2008

Low molecular mass polypeptides (LMP) 2 and LMP7 and transporter associated with antigen processing (TAP) subunits TAP1 and TAP2 play a crucial role in antigen processing and cell surface expression of HLA class I molecules. Since monoclonal antibodies (mAb) to these molecules will facilitate the analysis of their expression, structure and function in normal and transformed cells, in the present study we have developed these reagents. Specifically anti-LMP2 and LMP7 mAb were generated from BALB/c mice immunized with specific peptides, and anti-TAP1 and TAP2 mAb from BALB/c mice immunized with respective recombinant proteins. mAb VF101-39F7 and VF101-39G5 were shown to be specific for LMP2, …

Proteasome Endopeptidase Complexmedicine.drug_classRecombinant Fusion ProteinsImmunologyAntigen presentationBiologyMonoclonal antibodyBiochemistrylaw.inventionCell LineMicelawATP Binding Cassette Transporter Subfamily B Member 3Antibody SpecificityHLA AntigensMultienzyme ComplexesGeneticsmedicineImmunology and AllergyAnimalsHumansATP Binding Cassette Transporter Subfamily B Member 2DNA PrimersSkinAntigen PresentationMice Inbred BALB CHybridomasImmunoperoxidaseBase SequenceAntigen processingAntibodies MonoclonalProteinsGeneral MedicineTransporter associated with antigen processingMolecular biologyImmunohistochemistryCysteine EndopeptidasesCell cultureMonoclonalRecombinant DNAATP-Binding Cassette TransportersFemaleIndicators and ReagentsTissue antigens
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The Role of Low Complexity Regions in Protein Interaction Modes: An Illustration in Huntingtin

2021

Low complexity regions (LCRs) are very frequent in protein sequences, generally having a lower propensity to form structured domains and tending to be much less evolutionarily conserved than globular domains. Their higher abundance in eukaryotes and in species with more cellular types agrees with a growing number of reports on their function in protein interactions regulated by post-translational modifications. LCRs facilitate the increase of regulatory and network complexity required with the emergence of organisms with more complex tissue distribution and development. Although the low conservation and structural flexibility of LCRs complicate their study, evolutionary studies of proteins …

Protein Conformation alpha-Helical0301 basic medicineNetwork complexityHuntingtinintrinsically disordered regionsAmino Acid MotifsComputational biologyBiologyprotein interactionsArticlecompositionally biased regionsCatalysisProtein–protein interactionlcsh:ChemistryEvolution MolecularInorganic ChemistryLow complexity03 medical and health sciencesProtein DomainsProtein Interaction MappingAnimalsHumansp300-CBP Transcription FactorsAmino Acid SequenceProtein Interaction MapsHuntingtinTissue distributionPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopyHuntingtin Protein030102 biochemistry & molecular biologyOrganic ChemistryNuclear Proteinsp120 GTPase Activating ProteinGeneral MedicineMultiple modesSynapsinslow complexity regionsComputer Science ApplicationshomorepeatsMicroscopy Electron030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Sequence AlignmentFunction (biology)Protein BindingInternational Journal of Molecular Sciences
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Kinetic analysis and molecular modeling of the inhibition mechanism of roneparstat (SST0001) on human heparanase

2016

Heparanase is a β-d-glucuronidase which cleaves heparan sulfate chains in the extracellular matrix and on cellular membranes. A dysregulated heparanase activity is intimately associated with cell invasion, tumor metastasis and angiogenesis, making heparanase an attractive target for the development of anticancer therapies. SST0001 (roneparstat; Sigma-Tau Research Switzerland S.A.) is a non-anticoagulant 100% N-acetylated and glycol-split heparin acting as a potent heparanase inhibitor, currently in phase I in advanced multiple myeloma. Herein, the kinetics of heparanase inhibition by roneparstat is reported. The analysis of dose-inhibition curves confirmed the high potency of roneparstat (I…

Protein Conformation alpha-Helical0301 basic medicineSST0001Molecular modelhomology modelingAmino Acid MotifsPlasma protein bindingMolecular Dynamics SimulationBiochemistryMolecular Docking SimulationheparanaseSubstrate Specificity03 medical and health scienceschemistry.chemical_compound0302 clinical medicinePolysaccharidesHumansProtein Interaction Domains and MotifsHeparanaseHomology modelingEnzyme InhibitorsGlucuronidaseBinding Siteskinetic inhibition analysisHeparinComputational BiologyHeparan sulfateRecombinant ProteinsAcidobacteriaMolecular Docking SimulationEnzyme bindingKinetics030104 developmental biologyCarbohydrate SequenceFondaparinuxchemistryBiochemistryStructural Homology ProteinDocking (molecular)030220 oncology & carcinogenesisBiophysicsroneparstatThermodynamicsProtein Conformation beta-StrandORIGINAL ARTICLESProtein BindingGlycobiology
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A potential solution to avoid overdose of mixed drugs in the event of Covid-19: Nanomedicine at the heart of the Covid-19 pandemic.

2021

Since 2020, the world is facing the first global pandemic of 21st century. Among all the solutions proposed to treat this new strain of coronavirus, named SARS-CoV-2, the vaccine seems a promising way but the delays are too long to be implemented quickly. In the emergency, a dual therapy has shown its effectiveness but has also provoked a set of debates around the dangerousness of a particular molecule, hydroxychloroquine. In particular, the doses to be delivered, according to the studies, were well beyond the acceptable doses to support the treatment without side effects. We propose here to use all the advantages of nanovectorization to address this question of concentration. Using quantum…

Protein Conformation alpha-HelicalComputer science02 engineering and technologyAzithromycinDrug Delivery SystemsPandemicMaterials ChemistryDrug Dosage CalculationsSpectroscopymedia_common0303 health sciencesEvent (computing)021001 nanoscience & nanotechnologyComputer Graphics and Computer-Aided DesignMolecular Docking SimulationNanomedicineRisk analysis (engineering)Spike Glycoprotein CoronavirusDensity functional theory calculationsNanomedicineThermodynamicsNitrogen OxidesAngiotensin-Converting Enzyme 20210 nano-technologyHydroxychloroquineProtein BindingDrugBoron CompoundsCoronavirus disease 2019 (COVID-19)media_common.quotation_subjectSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)Molecular Dynamics SimulationAntiviral AgentsArticle03 medical and health sciencesHumansProtein Interaction Domains and MotifsDual therapyPhysical and Theoretical Chemistry030304 developmental biologyDrug transportBinding SitesSARS-CoV-2Molecular dynamics simulationsCOVID-19NanostructuresCOVID-19 Drug TreatmentKineticsQuantum TheoryProtein Conformation beta-StrandNanovectorizationJournal of molecular graphicsmodelling
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Extracellular loop 2 of G protein-coupled olfactory receptors is critical for odorant recognition

2021

International audience; G protein-coupled olfactory receptors (ORs) enable us to detect innumerous odorants. They are also ectopically expressed in non-olfactory tissues and emerging as attractive drug targets. ORs can be promiscuous or highly specific, which is part of a larger mechanism for odor discrimination. Here, we demonstrate that the OR extracellular loop 2 (ECL2) plays critical roles in OR promiscuity and specificity. Using site-directed mutagenesis and molecular modeling, we constructed 3D OR models in which ECL2 forms a lid over the orthosteric pocket. We demonstrate using molecular dynamics simulations that ECL2 controls the shape and the volume of the odorant-binding pocket, m…

Protein Conformation alpha-HelicalOdorant bindingG protein[SDV]Life Sciences [q-bio]Mutagenesis (molecular biology technique)Molecular Dynamics SimulationLigandsReceptors OdorantBiochemistryMice[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyExtracellularOlfactory receptorAnimalsHumans[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyReceptorMolecular BiologyG protein-coupled receptorVirtual screeningmolecular modelingChemistryCell Biologyvirtual screeningLigand (biochemistry)Cell biology[SDV] Life Sciences [q-bio]Smell[SDV.AEN] Life Sciences [q-bio]/Food and NutritionOdorantsMutagenesis Site-Directedsite-directed mutagenesis[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition
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The molecular heterogeneity of hemocyanin: Structural and functional properties of the 4×6-meric protein of Upogebia pusilla (Crustacea)

2006

The structural properties of the hemocyanin isolated from the Mediterranean mud shrimp, Upogebia pusilla (Decapoda: Thalassinidea), were investigated. Our intent was to make use of the U. pusilla case to perform a structural comparison between crustacean and chelicerate 4×6-meric hemocyanins. The thalassinidean hemocyanin appears similar in size but different in structural organization compared to the chelicerate 4×6-mer. Ultracentrifuge analyses on the purified protein revealed a sedimentation coefficient of 39S, typical of 4×6 hemocyanins. Electron micrographs are in agreement with a model in which four 2×6-meric building blocks are arranged in a tetrahedron-like quaternary structure and …

Protein Conformation030310 physiologymedicine.medical_treatmentAllosteric regulationHemocyaninDivalent03 medical and health sciencesOxygen bindingDecapodaCatalytic propertiesGeneticsmedicineQuaternary structureAnimals030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyDecapodaHemocyaninGeneral Medicinebiology.organism_classificationHemocyanin; Quaternary structure; Dissociation; Oxygen binding; Catalytic propertiesMolecular WeightOxygenSedimentation coefficientMicroscopy ElectronchemistryBiochemistryHemocyaninsChromatography GelProtein quaternary structureUltracentrifugeDissociationOxygen bindingProtein BindingGene
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