Search results for "recombinant"

showing 10 items of 1150 documents

Activation of EDTA-resistant Gelatinases in Malignant Human Tumors

2006

Abstract Among the many proteases associated with human cancer, seprase or fibroblast activation protein α, a type II transmembrane glycoprotein, has two types of EDTA-resistant protease activities: dipeptidyl peptidase and a 170-kDa gelatinase activity. To test if activation of gelatinases associated with seprase could be involved in malignant tumors, we used a mammalian expression system to generate a soluble recombinant seprase (r-seprase). In the presence of putative EDTA-sensitive activators, r-seprase was converted into 70- to 50-kDa shortened forms of seprase (s-seprase), which exhibited a 7-fold increase in gelatinase activity, whereas levels of dipeptidyl peptidase activity remaine…

Models MolecularCancer ResearchProteasesProtein ConformationDipeptidyl-peptidase activityIn situ hybridizationBiologyDipeptidyl peptidaseArticleCell LineFibroblast activation protein alphaNeoplasmsEndopeptidasesmedicineGelatinaseAnimalsHumansDipeptidyl-Peptidases and Tripeptidyl-PeptidasesEdetic AcidSerine EndopeptidasesMembrane ProteinsHaplorhinimedicine.diseaseRecombinant Proteinsseprase fibroblast activation protein alpha (FAP-α) gelatinase activation malignant tumorEnzyme ActivationOncologyBiochemistryGelatinasesCancer researchImmunohistochemistryAdenocarcinoma
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The Escherichia coli Envelope Stress Sensor CpxA Responds to Changes in Lipid Bilayer Properties

2015

The Cpx stress response system is induced by various environmental and cellular stimuli. It is also activated in Escherichia coli strains lacking the major phospholipid, phosphatidylethanolamine (PE). However, it is not known whether CpxA directly senses changes in the lipid bilayer or the presence of misfolded proteins due to the lack of PE in their membranes. To address this question, we used an in vitro reconstitution system and vesicles with different lipid compositions to track modulations in the activity of CpxA in different lipid bilayers. Moreover, the Cpx response was validated in vivo by monitoring expression of a PcpxP-gfp reporter in lipid-engineered strains of E. coli. Our comb…

Models MolecularCardiolipinsSurface PropertiesRecombinant Fusion ProteinsGreen Fluorescent ProteinsLipid BilayersArabidopsisPhospholipidBiologymedicine.disease_causeBiochemistrychemistry.chemical_compoundBacterial ProteinsGenes ReportermedicineAcholeplasma laidlawiiPhosphorylationLipid bilayerEscherichia coliPlant ProteinsPhosphatidylethanolamineEscherichia coli ProteinsPhosphatidylethanolaminesVesicleGlycosyltransferasesMembrane ProteinsPhosphatidylglycerolsCell biologychemistryMembrane proteinlipids (amino acids peptides and proteins)Protein foldingSignal transductionProtein KinasesProtein Processing Post-TranslationalSignal TransductionBiochemistry
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The mechanism of binding staphylococcal protein A to immunoglobin G does not involve helix unwinding.

1996

Structural changes in staphylococcal protein A (SpA) upon its binding to the constant region (Fc) of immunoglobulin G (IgG) have been studied by nuclear magnetic resonance and circular dichroism (CD) spectroscopy. The NMR solution structure of the engineered IgG-binding domain of SpA, the Z domain (an analogue of the B domain of SpA), has been determined by simulated annealing with molecular dynamics, using 599 distance and dihedral angle constraints. Domain Z contains three alpha-helices in the polypeptide segments Lys7 to His18 (helix 1), Glu25 to Asp36 (helix 2), and Ser41 to Ala54 (helix 3). The overall chain fold is an antiparallel three-helical bundle. This is in contrast to the previ…

Models MolecularCircular dichroismProtein FoldingMagnetic Resonance SpectroscopyStereochemistryMolecular Sequence DataPlasma protein bindingDihedral angleBiochemistryProtein Structure SecondaryProtein structureComputer GraphicsAmino Acid SequenceBinding siteStaphylococcal Protein ABinding SitesChemistryCircular DichroismNuclear magnetic resonance spectroscopyRecombinant ProteinsImmunoglobulin Fc FragmentsModels StructuralCrystallographyIgG bindingImmunoglobulin GMutagenesis Site-DirectedProtein foldingProtein BindingBiochemistry
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Flexible Structure of Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21.

2015

Filamins (FLNs) are large, multidomain actin cross-linking proteins with diverse functions. Besides regulating the actin cytoskeleton, they serve as important links between the extracellular matrix and the cytoskeleton by binding cell surface receptors, functioning as scaffolds for signaling proteins, and binding several other cytoskeletal proteins that regulate cell adhesion dynamics. Structurally, FLNs are formed of an amino terminal actin-binding domain followed by 24 immunoglobulin-like domains (IgFLNs). Recent studies have demonstrated that myosin-mediated contractile forces can reveal hidden protein binding sites in the domain pairs IgFLNa18-19 and 20-21, enabling FLNs to transduce me…

Models MolecularDIMERIZATIONMagnetic Resonance SpectroscopyFilaminsProtein domainlcsh:MedicinePlasma protein bindingmacromolecular substancesBiologyMyosinsFilaminCrystallography X-RayLigandsfilaminsFORCEProtein structureAUTO-INHIBITIONBINDINGEscherichia coliCytoskeletonPHOSPHORYLATIONlcsh:ScienceCytoskeletonFRAGMENTMultidisciplinaryBinding Siteslcsh:Rta1182Signal transducing adaptor proteinfilamiinitSMALL-ANGLE SCATTERINGActin cytoskeletonActinsRecombinant ProteinsCell biologyProtein Structure TertiaryMODELBIOLOGICAL MACROMOLECULESCytoskeletal Proteinspeptiditpeptides1182 Biochemistry cell and molecular biologylcsh:QPeptidesINTEGRINBinding domainProtein BindingResearch ArticlePloS one
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Molecular dissection of human Argonaute proteins by DNA shuffling.

2013

A paramount task in RNA interference research is to decipher the complex biology of cellular effectors, exemplified in humans by four pleiotropic Argonaute proteins (Ago1-Ago4). Here, we exploited DNA family shuffling, a molecular evolution technology, to generate chimeric Ago protein libraries for dissection of intricate phenotypes independently of prior structural knowledge. Through shuffling of human Ago2 and Ago3, we discovered two N-terminal motifs that govern RNA cleavage in concert with the PIWI domain. Structural modeling predicts an impact on protein rigidity and/or RNA-PIWI alignment, suggesting new mechanistic explanations for Ago3's slicing deficiency. Characterization of hybrid…

Models MolecularDNA ComplementaryProtein ConformationRecombinant Fusion ProteinsMolecular Sequence DataDNA RecombinantPiwi-interacting RNASequence alignmentComputational biologyBiologyStructural BiologyMolecular evolutionRNA interferenceConsensus SequenceConsensus sequenceHumansAmino Acid SequenceEukaryotic Initiation FactorsRNA Processing Post-TranscriptionalRNA Small InterferingMolecular BiologyGene LibraryGeneticsSequence Homology Amino AcidRNADNA ShufflingArgonauteDNA shufflingProtein Structure TertiaryMicroRNAsPhenotypeArgonaute ProteinsRNA InterferenceDirected Molecular EvolutionSequence AlignmentNature structuralmolecular biology
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Insights into the catalytic mechanism of human sEH phosphatase by site-directed mutagenesis and LC-MS/MS analysis

2008

We have recently reported that human soluble epoxide hydrolase (sEH) is a bifunctional enzyme with a novel phosphatase enzymatic activity. Based on a structural relationship with other members of the haloacid dehalogenase superfamily, the sEH N-terminal phosphatase domain revealed four conserved sequence motifs, including the proposed catalytic nucleophile D9, and several other residues potentially implicated in substrate turnover and/or Mg(2+) binding. To enlighten the catalytic mechanism of dephosphorylation, we constructed sEH phosphatase active-site mutants by site-directed mutagenesis. A total of 18 mutants were constructed and recombinantly expressed in Escherichia coli as soluble pro…

Models MolecularEpoxide hydrolase 2Molecular Sequence DataPhosphatase10050 Institute of Pharmacology and Toxicology610 Medicine & healthMass SpectrometryPhosphatesDephosphorylation1315 Structural BiologyProtein structureStructural Biology1312 Molecular BiologyHumansPhosphofructokinase 2Amino Acid SequenceBinding siteProtein Structure QuaternarySite-directed mutagenesisMolecular BiologyEpoxide HydrolasesBinding SitesChemistrySubstrate (chemistry)Phosphoric Monoester HydrolasesRecombinant ProteinsProtein Structure TertiaryProtein SubunitsBiochemistryMutagenesis Site-Directed570 Life sciences; biologyDimerizationSequence AlignmentChromatography Liquid
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Asp333, Asp495, and His52.3 Form the Catalytic Triad of Rat Soluble Epoxide Hydrolase

1996

On the basis of the sequence similarity between mammalian epoxide hydrolases and bacterial haloalkane dehalogenase reported earlier (Arand, M., Grant, D. F., Beetham, J. K., Friedberg, T., Oesch, F., and Hammock, B. D. (1994) FEBS Lett. 338, 251-256; Beetham, J. K., Grant, D., Arand, M., Garbarino, J., Kiyosue, T., Pinot, F., Oesch, F., Belknap, W. R., Shinozaki, K., and hammock, B. D. (1995) DNA Cell. Biol. 14, 61-71) we selected candidate amino acid residues for the putative catalytic triad of the rat soluble epoxide hydrolase. The predicted amino acid residues were exchanged by site-directed mutagenesis of the epoxide hydrolase cDNA, followed by the expression of the respective mutant en…

Models MolecularEpoxide hydrolase 2StereochemistryMolecular Sequence DataRestriction MappingPolymerase Chain ReactionBiochemistryCatalysisProtein Structure SecondaryCatalytic triadEscherichia coliAnimalsHumansPoint MutationHistidineAmino Acid SequenceCloning MolecularEpoxide hydrolaseMolecular BiologyPeptide sequenceDNA PrimersEpoxide Hydrolaseschemistry.chemical_classificationAspartic AcidBinding SitesSequence Homology Amino AcidChemistryCell BiologyRecombinant ProteinsRatsAmino acidEpoxide hydrolase activityKineticsBiochemistryEpoxide HydrolasesMutagenesis Site-DirectedHaloalkane dehalogenaseJournal of Biological Chemistry
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Optical properties of in-vitro biomineralised silica

2012

Silicon is the second most common element on the Earth's crust and its oxide (SiO(2)) the most abundant mineral. Silica and silicates are widely used in medicine and industry as well as in micro- and nano-optics and electronics. However, the fabrication of glass fibres and components requires high temperature and non-physiological conditions, in contrast to biosilica structures in animals and plants. Here, we show for the first time the use of recombinant silicatein-α, the most abundant subunit of sponge proteins catalyzing biosilicification reactions, to direct the formation of optical waveguides in-vitro through soft microlithography. The artificial biosilica fibres mimic the natural spon…

Models MolecularFabricationMaterials scienceOptical fiberSiliconProtein ConformationOxidechemistry.chemical_elementNanotechnologyArticlelaw.inventionchemistry.chemical_compoundSponge spiculelawAnimalsFiber Optic TechnologyMultidisciplinarybiologybiology.organism_classificationCathepsinsRecombinant ProteinsSpongechemistryCommon elementGlassRefractive index
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Molecular dynamics studies on HIV-1 protease: a comparison of the flap motions between wild type protease and the M46I/G51D double mutant

2007

The emergence of drug-resistant mutants of HIV-1 is a tragic effect associated with conventional long-treatment therapies against acquired immunodeficiency syndrome. These mutations frequently involve the aspartic protease encoded by the virus; knowledge of the molecular mechanisms underlying the conformational changes of HIV-1 protease mutants may be useful in developing more effective and longer lasting treatment regimes. The flap regions of the protease are the target of a particular type of mutations occurring far from the active site. These mutations modify the affinity for both substrate and ligands, thus conferring resistance. In this work, molecular dynamics simulations were perform…

Models MolecularGromacs 3.2Anti-HIV AgentsProtein Conformationmedicine.medical_treatmentflap motionMutantCatalysisVirusInorganic ChemistryProtein structureHIV ProteaseHIV-1 proteaseDrug Resistance ViralEnzyme StabilityHIV-1 proteasemedicineHumansComputer SimulationPhysical and Theoretical Chemistrychemistry.chemical_classificationProteasebiologyHIV-1 drug-resistant mutantOrganic ChemistryWild typeActive siteRecombinant ProteinsComputer Science ApplicationsCell biologyEnzymemolecular dynamics simulationAmino Acid SubstitutionComputational Theory and MathematicsBiochemistrychemistryMutationHIV-1biology.protein
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Molecular and structural characterization of fluorescent human parvovirus B19 virus-like particles

2005

Although sharing a T = 1 icosahedral symmetry with other members of the Parvoviridae family, it has been suggested that the fivefold channel of the human parvovirus B19 VP2 capsids is closed at its outside end. To investigate the possibility of placing a relatively large protein moiety at this site of B19, fluorescent virus-like particles (fVLPs) of B19 were developed. The enhanced green fluorescent protein (EGFP) was inserted at the N-terminus of the structural protein VP2 and assembly of fVLPs from this fusion protein was obtained. Electron microscopy revealed that these fluorescent protein complexes were very similar in size when compared to wild-type B19 virus. Further, fluorescence cor…

Models MolecularImmunoprecipitationRecombinant Fusion ProteinsvirusesGreen Fluorescent ProteinsBiophysicsFluorescence correlation spectroscopyEndosomesSpodopteraBiologyMicroscopy Atomic ForceBiochemistryFluorescenceCell LineGreen fluorescent proteinParvoviridae InfectionsBimolecular fluorescence complementationCell Line Tumorhemic and lymphatic diseasesParvovirus B19 HumanAnimalsHumansImmunoprecipitationMolecular BiologyParvoviridaeImmune SeraVirus AssemblyVirionvirus diseasesCell Biologybiology.organism_classificationFusion proteinMolecular biologyNanostructuresCell biologyTransport proteinProtein TransportCapsidCapsid Proteins
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