Search results for "binding"

showing 10 items of 3896 documents

Investigation of protein folding by coarse-grained molecular dynamics with the UNRES force field.

2010

Coarse-grained molecular dynamics simulations offer a dramatic extension of the time-scale of simulations compared to all-atom approaches. In this article, we describe the use of the physics-based united-residue (UNRES) force field, developed in our laboratory, in protein-structure simulations. We demonstrate that this force field offers about a 4000-times extension of the simulation time scale; this feature arises both from averaging out the fast-moving degrees of freedom and reduction of the cost of energy and force calculations compared to all-atom approaches with explicit solvent. With massively parallel computers, microsecond folding simulation times of proteins containing about 1000 r…

Protein FoldingStaphylococcus aureusRotationMolecular Dynamics SimulationKinetic energyForce field (chemistry)Protein Structure SecondaryArticleMolecular dynamicsMiceProtein structureBacterial ProteinsComputational chemistryAnimalsStatistical physicsPhysical and Theoretical ChemistryMassively parallelQuantitative Biology::BiomoleculesPrincipal Component AnalysisModels StatisticalChemistryProteinsMicrosecondKineticsBundleSolventsThermodynamicsProtein foldingTranscriptional Elongation FactorsCarrier ProteinsAlgorithmsProtein BindingThe journal of physical chemistry. A
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Calcium negatively regulates meprin β activity and attenuates substrate cleavage

2015

The meprin β metalloproteinase is an important enzyme in extracellular matrix turnover, inflammation, and neurodegeneration in humans and mice. Previous studies showed a diminished cleavage of certain meprin β substrates in the presence of calcium, although the mechanism was not clear. With the help of a specific fluorogenic peptide assay and the human amyloid precursor protein as substrate, we demonstrated that the influence of calcium is most likely a direct effect on human meprin β itself. Analyzing the crystal structures of pro- and mature meprin β helped to identify a cluster of negatively charged amino acids forming a potential calcium binding site. Mutation of 2 of these residues (D2…

Protein Foldingchemistry.chemical_elementCalciumEndoplasmic ReticulumBiochemistryCell LineSubstrate SpecificityAmyloid beta-Protein PrecursorChlorocebus aethiopsGeneticsAmyloid precursor proteinAnimalsHumansAmino Acid SequenceBinding siteProtein precursorMolecular BiologyCellular localizationSecretory pathwayMetalloproteinaseAmyloid beta-PeptidesBinding SitesbiologyEndoplasmic reticulumMetalloendopeptidasesCell biologyHEK293 CellschemistryCOS CellsMutationMetalloproteasesbiology.proteinCalciumAmyloid Precursor Protein SecretasesSequence AlignmentBiotechnologyThe FASEB Journal
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Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia

2019

Mitral valve diseases affect approximately 3% of the population and are the most common reasons for valvular surgery because no drug-based treatments exist. Inheritable genetic mutations have now been established as the cause of mitral valve insufficiency, and four different missense mutations in the filamin A gene (FLNA) have been found in patients suffering from non-syndromic mitral valve dysplasia (MVD). The FLNA protein is expressed, in particular, in endocardial endothelia during fetal valve morphogenesis and is key in cardiac development. The FLNA-MVD causing mutations are clustered in the N-terminal region of FLNA. How the mutations in FLNA modify its structure and function, have mos…

Protein FoldingdysplasiatFilamins[SDV]Life Sciences [q-bio]PopulationProtein Tyrosine Phosphatase Non-Receptor Type 12BiophysicsMutation Missensesynnynnäiset sydänviatProtein tyrosine phosphataseBiologyMolecular Dynamics Simulationmedicine.disease_causeFilamin03 medical and health sciences0302 clinical medicinemitral valve dysplasiaMitral valvemedicineFLNAMissense mutationHumanseducationGene030304 developmental biologyGenetics0303 health sciencesMutationeducation.field_of_studyBinding SitesMitral Valve Prolapsecritical structural defectshiippaläppäfilamiinitArticles3. Good healthmedicine.anatomical_structurecardiovascular systemfilamin A mutationsgeneettiset tekijätmutaatiot030217 neurology & neurosurgeryProtein Binding
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Different protein turnover of interleukin-6-type cytokine signalling components.

1999

Interleukin (IL)-6 and IL-6-type cytokines signal through the gp130/Jak/STAT signal transduction pathway. The key components involved are the signal transducing receptor subunit gp130, the Janus kinases Jak1, Jak2 and Tyk2, STAT1 and STAT3 of the family of signal transducers and activators of transcription, the protein tyrosine phosphatase SHP2 and the suppressors of cytokine signalling SOCS1, SOCS2 and SOCS3. Whereas considerable information has been accumulated concerning the time-course of activation for the individual signalling molecules, data on the availability of the proteins involved in IL-6-type cytokine signal transduction are scarce. Nevertheless, availability of these molecules…

Protein Tyrosine Phosphatase Non-Receptor Type 11Protein tyrosine phosphataseBiologyBiochemistrySuppressor of cytokine signallingAntigens CDCytokine Receptor gp130Membrane GlycoproteinsSuppressor of cytokine signaling 1Interleukin-6Protein Tyrosine Phosphatase Non-Receptor Type 6Intracellular Signaling Peptides and ProteinsJAK-STAT signaling pathwaySignal transducing adaptor proteinSTAT2 Transcription FactorProtein-Tyrosine KinasesGlycoprotein 130Recombinant ProteinsCell biologyDNA-Binding ProteinsSTAT1 Transcription FactorBiochemistryTrans-ActivatorsCytokinesSignal transductionProtein Tyrosine PhosphatasesJanus kinaseHalf-LifeSignal TransductionEuropean journal of biochemistry
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Targeting SARS-CoV-2 RBD Interface: a Supervised Computational Data-Driven Approach to Identify Potential Modulators

2020

Coronavirus disease 2019 (COVID-19) has spread out as a pandemic threat affecting over 2 million people. The infectious process initiates via binding of SARS-CoV-2 Spike (S) glycoprotein to host angiotensin-converting enzyme 2 (ACE2). The interaction is mediated by the receptor-binding domain (RBD) of S glycoprotein, promoting host receptor recognition and binding to ACE2 peptidase domain (PD), thus representing a promising target for therapeutic intervention. Herein, we present a computational study aimed at identifying small molecules potentially able to target RBD. Although targeting PPI remains a challenge in drug discovery, our investigation highlights that interaction between SARS-CoV…

Protein domainPneumonia ViralDruggabilityDrug Evaluation Preclinicalprotein-protein interactionsComputational biologyBiologyMolecular Dynamics SimulationPeptidyl-Dipeptidase AMolecular dynamics01 natural sciencesBiochemistryMolecular Docking SimulationAntiviral Agentsdockingmolecular dynamicProtein–protein interactionSmall Molecule LibrariesBetacoronavirusProtein DomainsDrug DiscoveryHumansGeneral Pharmacology Toxicology and PharmaceuticsPandemicsPharmacologyFull Paperpharmacophore010405 organic chemistryDrug discoverySARS-CoV-2Organic ChemistryCOVID-19Small molecule0104 chemical sciencesProtein-Protein InteractionMolecular Docking Simulation010404 medicinal & biomolecular chemistryDocking (molecular)Spike Glycoprotein CoronavirusdockingMolecular MedicineAngiotensin-Converting Enzyme 2PharmacophoreCoronavirus InfectionsProtein Binding
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Linked Analysis of Large Cooperative, Allosteric Systems: The Case of the Giant HBL Hemoglobins

2008

Homotropic and heterotropic allosteric interactions are important mechanisms that regulate protein function. These mechanisms depend on the ability of oligomeric protein complexes to adopt different conformations and to transmit conformation-linked signals from one subunit of the complex to the neighboring ones. An important step in understanding the regulation of protein function is to identify and characterize the conformations available to the protein complex. This task becomes increasingly challenging with increasing numbers of interacting binding sites. However, a large number of interacting binding sites allows for high homotropic interactions (cooperativity) and thus represents the m…

Protein functionOrder (biology)BiochemistryHexagonal crystal systemBilayerProtein subunitAllosteric regulationBiophysicsCooperativityBiologyBinding site
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Drosophila Muscleblind Is Involved in troponin T Alternative Splicing and Apoptosis

2008

Background: Muscleblind-like proteins (MBNL) have been involved in a developmental switch in the use of defined cassette exons. Such transition fails in the CTG repeat expansion disease myotonic dystrophy due, in part, to sequestration of MBNL proteins by CUG repeat RNA. Four protein isoforms (MblA-D) are coded by the unique Drosophila muscleblind gene. Methodology/Principal Findings: We used evolutionary, genetic and cell culture approaches to study muscleblind (mbl) function in flies. The evolutionary study showed that the MblC protein isoform was readily conserved from nematods to Drosophila, which suggests that it performs the most ancestral muscleblind functions. Overexpression of MblC…

Protein isoformGenetics and Genomics/Animal GeneticsScienceAmino Acid MotifsRNA-binding proteinApoptosisBiology03 medical and health sciencesExon0302 clinical medicineTroponin TAnimalsDrosophila ProteinsGenetics and Genomics/Genetics of Disease030304 developmental biologyGenetics0303 health sciencesMultidisciplinaryQAlternative splicingRRNA-Binding ProteinsAlternative SplicingGenetics and Genomics/Disease ModelsRNA splicingMedicineDrosophilaTNNT3Trinucleotide Repeat Expansion030217 neurology & neurosurgeryDrosophila ProteinGenèticaMinigeneResearch Article
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Probing the Paradigm of Promiscuity for N‐Heterocyclic Carbene Complexes and their Protein Adduct Formation

2021

Metal complexes can be considered a "paradigm of promiscuity" when it comes to their interactions with proteins. They often form adducts with a variety of donor atoms in an unselective manner. We have characterized the adducts formed between a series of isostructural N-heterocyclic carbene (NHC) complexes with Ru, Os, Rh, and Ir centers and the model protein hen egg white lysozyme by X-ray crystallography and mass spectrometry. Distinctive behavior for the metal compounds was observed with the more labile Ru and Rh complexes targeting mainly a surface l-histidine moiety through cleavage of p-cymene or NHC co-ligands, respectively. In contrast, the more inert Os and Ir derivatives were detec…

Protein mass spectrometryStereochemistryBioorganometallic chemistryGeneral ChemistryGeneral MedicineLigand (biochemistry)CatalysisAdductchemistry.chemical_compoundchemistryMoietyIsostructuralBinding siteCarbeneAngewandte Chemie
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Recombinant functional multidomain hemoglobin from the gastropod Biomphalaria glabrata

2011

The extracellular hemoglobin multimer of the planorbid snail Biomphalaria glabrata, intermediate host of the human parasite Schistosoma mansoni, is presumed to be a 1.44 MDa complex of six 240 kDa polypeptide subunits, arranged as three disulfide-bridged dimers. The complete amino acid sequence of two subunit types (BgHb1 and BgHb2), and the partial sequence of a third type (BgHb3) are known. Each subunit encompasses 13 paralogus heme domains, and N-terminally a smaller plug domain responsible for subunit dimerization. We report here the recombinant expression of different functional fragments of BgHb2 in Escherichia coli, and of the complete functional subunits BgHb1 and BgHb2 in insect ce…

Protein subunitClinical BiochemistryCooperativitymedicine.disease_causeBiochemistrylaw.inventionHemoglobinschemistry.chemical_compoundlawGeneticsmedicineAnimalsHumansBiomphalaria glabrataProtein Structure QuaternaryMolecular BiologyEscherichia coliPeptide sequenceHemeBiomphalariabiologySchistosoma mansoniCell Biologybiology.organism_classificationRecombinant ProteinsOxygenProtein SubunitsBiochemistrychemistryRecombinant DNAOxygen bindingIUBMB Life
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Proteins participating to the post-transcriptional regulation of the mitochondrial cytochrome c oxidase subunit IV via elements located in the 3′UTR

2009

Abstract In developing rat brain cytochrome c oxidase subunit IV (COXIV) expression is also regulated at post-transcriptional level and two 3′UTR-COXIV RNA-binding factors have been identified. Here, we report the enrichment and identification of the factors from just born rat brains by affinity chromatography of biotinylated 3′UTR-COXIV RNA–protein complexes on streptavidin-conjugated paramagnetic particles. We successfully isolated two main proteins of about 86 and 42 kDa, whose sequences were highly attributable to Hsp90 and Actin. The purified proteins maintain RNA-binding ability and specificity for COXIV messenger and, interacting with the 3′UTR, then could negatively modulate mRNA tr…

Protein subunitRNA-binding proteinMitochondrionChromatography AffinityElectron Transport Complex IVMitochondrial ProteinsRats Sprague-DawleySequence Analysis ProteinSerineAnimalsCytochrome c oxidaseHSP90 Heat-Shock ProteinsPhosphorylationPost-transcriptional regulation RNA-binding proteins Mitochondria Cytochrome c oxidase COXIV 3'UTR3' Untranslated RegionsMolecular BiologyPost-transcriptional regulationMessenger RNAbiologyThree prime untranslated regionBrainRNA-Binding ProteinsTranslation (biology)Cell BiologyActinsRatsMolecular WeightAnimals NewbornGene Expression RegulationBiochemistrybiology.proteinMolecular MedicineProtein BindingMitochondrion
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