Search results for "Interaction"

showing 10 items of 5710 documents

A Computational Study of the Protein-Ligand Interactions in CDK2 Inhibitors: Using Quantum Mechanics/Molecular Mechanics Interaction Energy as a Pred…

2006

ABSTRACT: We report a combined quantum mechanics/molecular mechanics (QM/MM) study to determine the protein-ligand interaction energy between CDK2 (cyclin-dependent kinase 2) and five inhibitors with the N2 -substituted 6-cyclohexylmethoxypurine scaffold. The computational results in this work show that the QM/MM interaction energy is strongly correlated to the biological activity and can be used as a predictor, at least within a family of substrates. A detailed analysis of the protein-ligand structures obtained from molecular dynamics simulations shows specific interactions within the active site that, in some cases, have not been reported before to our knowledge. The computed interaction …

Models MolecularWork (thermodynamics)Protein ConformationBiophysicsBiophysical Theory and ModelingMechanicsMolecular mechanicssymbols.namesakeMolecular dynamicsProtein structureSimulación por ComputadorDiseño de FármacosModelos QuímicosUnión ProteicaQuantum mechanicsModelos MolecularesConformación ProteicaComputer SimulationProtein Kinase InhibitorsBinding SitesbiologyChemistryCyclin-Dependent Kinase 2Active siteInteraction energyModels ChemicalPurinesDrug Designsymbolsbiology.proteinQuantum Theoryvan der Waals forceQuinasa 2 Dependiente de la CiclinaProtein BindingProtein ligandBiophysical Journal
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Structure of the human filamin A actin-binding domain.

2009

Filamin A (FLNa) is a large dimeric protein that binds to actin filaments via its actin-binding domain (ABD). The crystal structure of this domain was solved at 3.2 A resolution. The domain adopts a closed conformation typical of other ABDs, but also forms a dimer both in crystallization conditions and in solution. The structure shows the localization of the residues mutated in patients with periventricular nodular heterotopia or otopalatodigital syndrome. Structural analysis predicts that mutations in both types of disorder may affect actin binding.

Models Molecularanimal structuresDimerFilaminsmacromolecular substancesFilaminCalponin homology domainCrystallography X-Raychemistry.chemical_compoundContractile ProteinsStructural BiologyFLNAHumansProtein Interaction Domains and MotifsActin-binding proteinProtein Structure QuaternaryActinbiologyMicrofilament ProteinsGeneral MedicineActinschemistryStructural Homology ProteinDomain (ring theory)Mutationbiology.proteinBiophysicsBinding domainProtein BindingActa crystallographica. Section D, Biological crystallography
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Interaction of Circadian Clock Proteins CRY1 and PER2 Is Modulated by Zinc Binding and Disulfide Bond Formation

2014

SummaryPeriod (PER) proteins are essential components of the mammalian circadian clock. They form complexes with cryptochromes (CRY), which negatively regulate CLOCK/BMAL1-dependent transactivation of clock and clock-controlled genes. To define the roles of mammalian CRY/PER complexes in the circadian clock, we have determined the crystal structure of a complex comprising the photolyase homology region of mouse CRY1 (mCRY1) and a C-terminal mouse PER2 (mPER2) fragment. mPER2 winds around the helical mCRY1 domain covering the binding sites of FBXL3 and CLOCK/BMAL1, but not the FAD binding pocket. Our structure revealed an unexpected zinc ion in one interface, which stabilizes mCRY1-mPER2 int…

Models Molecularendocrine systemanimal structuresPeriod (gene)Molecular Sequence DataCircadian clockBiologyCrystallography X-RayGeneral Biochemistry Genetics and Molecular BiologyMiceCryptochromeAnimalsProtein Interaction Domains and MotifsAmino Acid SequenceCircadian rhythmBinding siteBiochemistry Genetics and Molecular Biology(all)F-Box ProteinsPeriod Circadian ProteinsRecombinant ProteinsCryptochromesPER2ZincBiochemistryFAD bindingBiophysicsPeriod Circadian ProteinsSequence AlignmentCell
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Experimental and theoretical NMR studies of interaction between phenylalanine derivative and egg yolk lecithin

2014

The interaction of phenylalanine diamide (Ac-Phe-NHMe) with egg yolk lecithin (EYL) in chloroform was studied by 1H and 13C NMR. Six complexes EYL–Ac-Phe-NHMe, stabilized by N–H···O or/and C–H···O hydrogen bonds, were optimized at M06-2X/6-31G(d,p) level. The assignment of EYL and Ac-Phe-NHMe NMR signals was supported using GIAO (gauge including atomic orbital) NMR calculations at VSXC and B3LYP level of theory combined with STO-3Gmag basis set. Results of our study indicate that the interaction of peptides with lecithin occurs mainly in the polar ‘head’ of the lecithin. Additionally, the most probable lecithin site of H-bond interaction with Ac-Phe-NHMe is the negatively charged oxygen in …

Models Molecularfood.ingredientMagnetic Resonance SpectroscopyPhenylalanineMolecular ConformationPhenylalanineLecithinDFTchemistry.chemical_compoundfoodYolkLecithinsMaterials TestingOrganic chemistryAnimalsGeneral Materials ScienceComputer Simulationhydrogen bondChloroformBinding Sitesintermolecular interactionsHydrogen bondIntermolecular forceGeneral ChemistryCarbon-13 NMREgg YolkpeptideNMR3. Good healthCrystallographylecithinchemistryModels ChemicalChickensDerivative (chemistry)Magnetic Resonance in Chemistry
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The C-terminal rod 2 fragment of filamin A forms a compact structure that can be extended

2012

Filamins are large proteins that cross-link actin filaments and connect to other cellular components. The C-terminal rod 2 region of FLNa (filamin A) mediates dimerization and interacts with several transmembrane receptors and intracellular signalling adaptors. SAXS (small-angle X-ray scattering) experiments were used to make a model of a six immunoglobulin-like domain fragment of the FLNa rod 2 (domains 16–21). This fragment had a surprising three-branched structural arrangement, where each branch was made of a tightly packed two-domain pair. Peptides derived from transmembrane receptors and intracellular signalling proteins induced a more open structure of the six domain fragment. Mutagen…

Models Moleculargenetics [Receptors Dopamine D3]metabolism [Recombinant Proteins]Protein Conformationgenetics [Antigens CD18]chemistry [Recombinant Proteins]Plasma protein bindingCrystallography X-RayLigandsFilaminmetabolism [Antigens CD18]metabolism [Cytoskeletal Proteins]BiochemistryfilaminsContractile ProteinsProtein structuremetabolism [Peptide Fragments]FLNAchemistry [Antigens CD18]genetics [Cell Adhesion Molecules]Small-angle X-ray scatteringMicrofilament Proteinsgenetics [Contractile Proteins]Recombinant Proteinschemistry [Receptors Dopamine D3]FBLIM1 protein humanddc:540Domain (ring theory)DimerizationProtein Bindingchemistry [Contractile Proteins]FilaminsAntigens CD18metabolism [Cell Adhesion Molecules]BiologyScattering Small Anglemetabolism [Receptors Dopamine D3]Humanschemistry [Microfilament Proteins]Protein Interaction Domains and Motifsmetabolism [Mutant Proteins]DRD3 protein humanMolecular Biologymetabolism [Contractile Proteins]Actingenetics [Cytoskeletal Proteins]Cryoelectron MicroscopyMutagenesista1182Receptors Dopamine D3metabolism [Microfilament Proteins]Cell Biologychemistry [Cell Adhesion Molecules]genetics [Peptide Fragments]Peptide FragmentsCytoskeletal ProteinsCrystallographychemistry [Mutant Proteins]chemistry [Peptide Fragments]CD18 AntigensBiophysicschemistry [Cytoskeletal Proteins]Mutant Proteinsgenetics [Microfilament Proteins]Cell Adhesion MoleculesBiochemical Journal
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The Minor Capsid Protein VP11 of Thermophilic Bacteriophage P23-77 Facilitates Virus Assembly by Using Lipid-Protein Interactions

2015

ABSTRACT Thermus thermophilus bacteriophage P23-77 is the type member of a new virus family of icosahedral, tailless, inner-membrane-containing double-stranded DNA (dsDNA) viruses infecting thermophilic bacteria and halophilic archaea. The viruses have a unique capsid architecture consisting of two major capsid proteins assembled in various building blocks. We analyzed the function of the minor capsid protein VP11, which is the third known capsid component in bacteriophage P23-77. Our findings show that VP11 is a dynamically elongated dimer with a predominantly α-helical secondary structure and high thermal stability. The high proportion of basic amino acids in the protein enables electrost…

Models MolecularvirusesMolecular Sequence DataStatic ElectricityImmunologyMicrobiologyProtein–protein interactionBacteriophagechemistry.chemical_compoundCapsidVirologyBacteriophagesAmino Acid SequenceThermusPeptide sequenceProtein secondary structureprotein-lipid systemsbiologyVirus AssemblyStructure and AssemblyCapsomereVirionThermus thermophilusLipid Metabolismbiology.organism_classificationLipidsMolecular biologychemistryCapsidInsect Sciencethermophilic virusesBiophysicsCapsid ProteinsDNAkapsidiJournal of Virology
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Pharmacology and safety of tofacitinib in ulcerative colitis.

2020

The use of Janus kinase (JAK) inhibitors is a new approach in the therapy of inflammatory diseases with immune base. Tofacitinib is one of these inhibitors targeting JAK1 and JAK3, and its efficacy has been demonstrated in the treatment of moderate to severe ulcerative colitis (UC). It is a small synthetic molecule administered orally, with a fast bioavailability and elimination rate, predictable pharmacokinetics and lack of immunogenicity, which are convenient characteristics for both efficacy and safety. This article reviews the pharmacological characteristics of tofacitinib and its safety profile.

Moderate to severePharmacologyHerpes ZosterArthritis Rheumatoid03 medical and health sciences0302 clinical medicineImmune systemPharmacokineticsPiperidinesNeoplasmsMedicineHerpes Zoster VaccineHumansJanus Kinase InhibitorsDrug InteractionsTofacitinibbusiness.industryImmunogenicityJanus Kinase 3Janus Kinase 1Venous Thromboembolismmedicine.diseaseUlcerative colitisBioavailabilityPyrimidines030220 oncology & carcinogenesis030211 gastroenterology & hepatologyColitis UlcerativeJanus kinasebusinessGastroenterologia y hepatologia
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The Modular X- and Gamma-Ray Sensor (MXGS)of the ASIM Payload on the International Space Station

2019

The Modular X- and Gamma-ray Sensor (MXGS) is an imaging and spectral X- and Gamma-ray instrument mounted on the starboard side of the Columbus module on the International Space Station. Together with the Modular Multi-Spectral Imaging Assembly (MMIA) (Chanrion et al. this issue) MXGS constitutes the instruments of the Atmosphere-Space Interactions Monitor (ASIM) (Neubert et al. this issue). The main objectives of MXGS are to image and measure the spectrum of X- and γ-rays from lightning discharges, known as Terrestrial Gamma-ray Flashes (TGFs), and for MMIA to image and perform high speed photometry of Transient Luminous Events (TLEs) and lightning discharges. With these two instruments sp…

Modular Multi-Spectral Imaging AssemblyPhysics - Instrumentation and Detectors010504 meteorology & atmospheric sciencesModular X- and Gamma-ray SensorFOS: Physical sciencesTerrestrial Gamma-ray FlashesInternational Space Station01 natural sciencesPhysics - Space Physics0103 physical sciencesInternational Space Station010303 astronomy & astrophysicsInstrumentation and Methods for Astrophysics (astro-ph.IM)Atmosphere-Space Interaction Monitor0105 earth and related environmental sciencesRemote sensingPhysicsbusiness.industryPayloadGamma rayX- and Gamma-ray detector for spaceAstronomy and AstrophysicsInstrumentation and Detectors (physics.ins-det)Modular designLightningSpace Physics (physics.space-ph)Photometry (astronomy)Space and Planetary ScienceTransient (oscillation)Astrophysics - Instrumentation and Methods for Astrophysicsbusiness
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Truncated internalin A and asymptomatic Listeria monocytogenes carriage: in vivo investigation by allelic exchange

2004

ABSTRACT Allelic exchange of the region coding for the C terminus of InlA between one epidemic (with an 80-kDa InlA) and one asymptomatic (with a 47-kDa InlA) carriage Listeria monocytogenes strain confirmed the need for this region for internalin entry in vitro. Interestingly, restoration of internalin A functionality did not result in full virulence in chicken embryo assays.

Molecular Sequence DataImmunologyVirulenceChick Embryomedicine.disease_causeMicrobiologyMicrobiology03 medical and health sciencesBacterial ProteinsListeria monocytogenesIn vivomedicineAnimalsHumansInternalinAlleleAlleles030304 developmental biology0303 health sciencesCellular Microbiology: Pathogen-Host Cell Molecular InteractionsBase SequenceVirulencebiology030306 microbiologyMicrobiology and Parasitologybacterial infections and mycosesbiology.organism_classificationListeria monocytogenesVirologyMicrobiologie et ParasitologieIn vitro3. Good healthInfectious DiseasesCarriage[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyParasitologyCaco-2 CellsBacteria
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The origin of Lecithodesmus (Digenea: Campulidae) based on ND3 gene comparison

2000

Species of Lecithodesmus (Campulidae) occur almost exclusively in baleen whales throughout a wide geographical distribution. Other campulids occur only in odontocetes and, secondarily, in pinnipeds and the sea otter. Therefore, the ancestor of Lecithodesmus might have either cospeciated with mysticetes during the early divergence of mysticete and odontocete cetaceans or originated later via host switching. We evaluate both possibilities based on a phylogenetic analysis. The ND3 mitochondrial gene sequence of a species of Lecithodesmus was included in a previous partial molecular phylogeny of the Campulidae. Fasciola hepatica and Dicrocoelium dendriticum were used as outgroups. Maximum parsi…

Molecular Sequence DataZoologyBiologyDNA MitochondrialDigeneaHost-Parasite InteractionsPhylogeneticsAdenine nucleotideAnimalsEcology Evolution Behavior and SystematicsPhylogenyLikelihood FunctionsPhylogenetic treeBase SequenceWhalesNADH DehydrogenaseSequence Analysis DNADNA Helminthbiology.organism_classificationMaximum parsimonyBaleenB vitaminsMolecular phylogeneticsParasitologyTrematodaSequence Alignment
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