Search results for "units"

showing 10 items of 576 documents

Complete subunit sequences, structure and evolution of the 6 x 6-mer hemocyanin from the common house centipede, Scutigera coleoptrata.

2003

Hemocyanins are large oligomeric copper-containing proteins that serve for the transport of oxygen in many arthropod species. While studied in detail in the Chelicerata and Crustacea, hemocyanins had long been considered unnecessary in the Myriapoda. Here we report the complete molecular structure of the hemocyanin from the common house centipede Scutigera coleoptrata (Myriapoda: Chilopoda), as deduced from 2D-gel electrophoresis, MALDI-TOF mass spectrometry, protein and cDNA sequencing, and homology modeling. This is the first myriapod hemocyanin to be fully sequenced, and allows the investigation of hemocyanin structure-function relationship and evolution. S. coleoptrata hemocyanin is a 6…

Models MolecularProtein Conformationmedicine.medical_treatmentMolecular Sequence DataMyriapodachemical and pharmacologic phenomenaBiochemistryEvolution MolecularMonophylymedicineAnimalsAmino Acid SequenceCloning MolecularArthropodsPhylogenybiologyMandibulatahemic and immune systemsHemocyaninAnatomybiology.organism_classificationProtein SubunitsEvolutionary biologyHemocyaninsChelicerataArthropodCentipedeSequence AlignmentScutigera coleoptrataEuropean journal of biochemistry
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Structure of Mega-Hemocyanin Reveals Protein Origami in Snails

2014

SummaryMega-hemocyanin is a 13.5 MDa oxygen transporter found in the hemolymph of some snails. Similar to typical gastropod hemocyanins, it is composed of 400 kDa building blocks but has additional 550 kDa subunits. Together, they form a large, completely filled cylinder. The structural basis for this highly complex protein packing is not known so far. Here, we report the electron cryomicroscopy (cryo-EM) structure of mega-hemocyanin complexes from two different snail species. The structures reveal that mega-hemocyanin is composed of flexible building blocks that differ in their conformation, but not in their primary structure. Like a protein origami, these flexible blocks are optimally pac…

Models MolecularProtein FoldingCryo-electron microscopymedicine.medical_treatmentGastropodaSnailsNanotechnologySnailBiologyMega-Cylinder (gastropod)Structural Biologybiology.animalHemolymphmedicineAnimalsProtein Structure QuaternaryMolecular BiologyCryoelectron MicroscopyProtein primary structureHemocyaninbiology.organism_classificationProtein SubunitsComplex proteinHemocyaninsBiophysicsProtein MultimerizationStructure
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Structural Characterization of Set1 RNA Recognition Motifs and their Role in Histone H3 Lysine 4 Methylation

2006

Departament de Bioquimica iBiologia Molecular, Universitatde Valencia, C/Dr Moliner 50,46100, Burjassot, SpainThe yeast Set1 histone H3 lysine 4 (H3K4) methyltransferase contains, inaddition to its catalytic SET domain, a conserved RNA recognition motif(RRM1). We present here the crystal structure and the secondary structureassignment in solution of the Set1 RRM1. Although RRM1 has the expectedβαββαβ RRM-fold, it lacks the typical RNA-binding features of thesemodules. RRM1 is not able to bind RNA by itself in vitro, but a constructcombining RRM1 with a newly identified downstream RRM2 specificallybinds RNA. Invivo,H3K4 methylation isnot affectedbyapoint mutation inRRM2 that preserves Set1 s…

Models MolecularRiboswitchHistone H3 Lysine 4Saccharomyces cerevisiae ProteinsRNA-induced transcriptional silencingSurface Properties[SDV]Life Sciences [q-bio]Molecular Sequence DataSaccharomyces cerevisiae[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]BiologyMethylationHistonesStructure-Activity Relationship03 medical and health sciencesStructural BiologyHistone methylation[SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Amino Acid SequenceProtein Structure QuaternaryMolecular BiologyConserved Sequence030304 developmental biology0303 health sciencesRNA recognition motifLysine030302 biochemistry & molecular biologyRNARNA FungalHistone-Lysine N-MethyltransferaseNon-coding RNAMolecular biology[SDV] Life Sciences [q-bio]DNA-Binding ProteinsProtein SubunitsBiochemistryHistone methyltransferaseSequence AlignmentProtein BindingTranscription Factors
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Controlling quaternary structure assembly: subunit interface engineering and crystal structure of dual chain avidin.

2006

Dual chain avidin (dcAvd) is an engineered avidin form, in which two circularly permuted chicken avidin monomers are fused into one polypeptide chain. DcAvd can theoretically form two different pseudotetrameric quaternary assemblies because of symmetry at the monomer-monomer interfaces. Here, our aim was to control the assembly of the quaternary structure of dcAvd. We introduced the mutation I117C into one of the circularly permuted domains of dcAvd and scanned residues along the 1-3 subunit interface of the other domain. Interestingly, V115H resulted in a single, disulfide locked quaternary assembly of dcAvd, whereas I117H could not guide the oligomerisation process even though it stabilis…

Models MolecularStereochemistryProtein subunitBiotinGene ExpressionCrystal structureCrystallography X-RayLigandsProtein EngineeringProtein–protein interactionchemistry.chemical_compoundBiotinStructural BiologyAnimalsDisulfidesProtein Structure QuaternaryMolecular BiologyChromatography High Pressure LiquidbiologyProtein engineeringHydrogen-Ion ConcentrationAvidinCrystallographyProtein SubunitsMonomerchemistryMutationbiology.proteinChromatography GelThermodynamicsProtein quaternary structureChickensAvidinJournal of molecular biology
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Meprins, membrane-bound and secreted astacin metalloproteinases

2008

The astacins are a subfamily of the metzincin superfamily of metalloproteinases. The first to be characterized was the crayfish enzyme astacin. To date more than 200 members of this family have been identified in species ranging from bacteria to humans. Astacins are involved in developmental morphogenesis, matrix assembly, tissue differentiation and digestion. Family members include the procollagen C-proteinase (BMP1, bone morphogenetic protein 1), tolloid and mammalian tolloid-like, HMP (Hydra vulgaris metalloproteinase), sea urchin BP10 (blastula protein) and SPAN (Strongylocentrotus purpuratus astacin), the 'hatching' subfamily comprising alveolin, ovastacin, LCE, HCE ('low' and 'high' c…

Models MolecularSubfamilyanimal structuresProtein ConformationClinical BiochemistryMolecular Sequence DataMatrix metalloproteinaseBiochemistryBone morphogenetic protein 1ArticleSubstrate SpecificityExtracellular matrixIntestinal mucosaAnimalsHumansTissue DistributionAmino Acid SequenceIntestinal MucosaMolecular BiologyPhylogenybiologyMetalloendopeptidasesGeneral Medicinebiology.organism_classificationStrongylocentrotus purpuratusMolecular biologyCell biologyProtein Subunitsembryonic structuresMolecular MedicineMATH domainAstacin
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Structural and functional consequences of the replacement of proximal residues Cys172 and Cys192 in the large subunit of ribulose-1,5-bisphosphate ca…

2008

Proximal Cys(172) and Cys(192) in the large subunit of the photosynthetic enzyme Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) are evolutionarily conserved among cyanobacteria, algae and higher plants. Mutation of Cys(172) has been shown to affect the redox properties of Rubisco in vitro and to delay the degradation of the enzyme in vivo under stress conditions. Here, we report the effect of the replacement of Cys(172) and Cys(192) by serine on the catalytic properties, thermostability and three-dimensional structure of Chlamydomonas reinhardtii Rubisco. The most striking effect of the C172S substitution was an 11% increase in the specificity factor when compared wi…

Models Molecularinorganic chemicalsOxygenaseRibulose-Bisphosphate CarboxylaseProtein subunitSpecificity factorChlamydomonas reinhardtiiCrystallography X-RayBiochemistryCatalysischemistry.chemical_compoundEnzyme StabilityAnimalsCysteineMolecular BiologyBinding SitesRibulose 15-bisphosphatebiologyfungiRuBisCOTemperaturefood and beveragesCell Biologybiology.organism_classificationLyaseMolecular biologyProtein Structure TertiaryPyruvate carboxylaseKineticsProtein SubunitsBiochemistrychemistryMutationbiology.proteinChlamydomonas reinhardtiiBiochemical Journal
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Effect of low-level GaAlAs laser irradiation on the proliferation rate of human periodontal ligament fibroblasts: an in vitro study

2003

Aim: The aim of this in vitro study was to evaluate a potential stimulatory effect of low-level laser irradiation on the proliferation of human periodontal ligament fibroblasts (PDLF). Materials and Methods: PDLF obtained from third molar periodontal ligaments were cultured under standard conditions and spread on 96-well tissue culture plates. Subconfluent monolayers were irradiated with an 809-nm diode laser operated at a power output of 10 mW in the continuos wave (cw) mode at energy fluences of 1.96‐7.84 Jcm ‐2 . The variable irradiation parameters were the time of exposure (75‐300 s per well) and the number of irradiations (1‐3). After laser treatment, the cultures were incubated for 24…

Molarbusiness.industryChemistrymedicine.medical_treatmentDentistryLaserMolecular biologylaw.inventionTissue cultureRelative fluorescence unitsCell culturelawmedicinePeriodonticsPeriodontal fiberIrradiationbusinessLow level laser therapyJournal of Clinical Periodontology
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Two α subunits and one β subunit of meprin zinc-endopeptidases are differentially expressed in the zebrafish Danio rerio

2007

Abstract Meprins are members of the astacin family of metalloproteases expressed in epithelial tissues, intestinal leukocytes and certain cancer cells. In mammals, there are two homologous subunits, which form complex glycosylated disulfide-bonded homo- and heterooligomers. Both human meprin α and meprin β cleave several basement membrane components, suggesting a role in epithelial differentiation and cell migration. There is also evidence that meprin β is involved in immune defence owing to its capability of activating interleukin-1β and the diminished mobility of intestinal leukocytes in meprin β-knockout mice. Here we show for the first time by reverse transcription PCR, immunoblotting a…

Molecular Sequence DataClinical BiochemistryDanioBiochemistryCatalysisChromosomesConserved sequenceAnimalsHumansAmino Acid SequenceRNA MessengerMolecular BiologyPeptide sequenceZebrafishConserved SequencePhylogenyZebrafishRegulation of gene expressionMessenger RNAbiologyMetalloendopeptidasesbiology.organism_classificationMolecular biologyProtein Structure TertiaryCell biologyProtein SubunitsZincGene Expression RegulationMicroscopy FluorescenceStructural Homology Proteinbiology.proteinAstacinSequence AlignmentATP synthase alpha/beta subunitsbchm
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Mapping of a binding site for ATP within the extracellular region of the Torpedo nicotinic acetylcholine receptor beta-subunit.

1997

Using 2,8,5'-[H-3]ATP as a direct photoaffinity label for membrane-bound nicotinic acetylcholine receptor (nAChR) from Torpedo marmorata, we have identified a binding site for ATP in the extracellular region of the beta-subunit of the receptor. Photolabeling was completely inhibited in the presence of saturating concentrations of nonradioactive ATP, whereas neither the purinoreceptor antagonists suramin, theophyllin, and caffeine nor the nAChR antagonists alpha-bungarotoxin and d-tubocurarine affected the labeling reaction. Competitive and noncompetitive nicotinic agonists and Ca2+ increased the yield of the photoreaction by up to 50%, suggesting that the respective binding sites are allost…

Molecular Sequence DataPhotoaffinity LabelsReceptors NicotinicTorpedoTritiumBiochemistryPeptide Mappingchemistry.chemical_compoundGanglion type nicotinic receptorAdenosine TriphosphateAdenine nucleotideAnimalsChymotrypsinTrypsinAmino Acid SequenceBinding siteBinding SitesbiologyHydrolysisCell MembranePeptide FragmentsNicotinic acetylcholine receptorNicotinic agonistBiochemistrychemistrybiology.proteinAlpha-4 beta-2 nicotinic receptorExtracellular SpaceAdenosine triphosphateSequence AnalysisATP synthase alpha/beta subunitsBiochemistry
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Real-Time Monocular Segmentation and Pose Tracking of Multiple Objects

2016

We present a real-time system capable of segmenting multiple 3D objects and tracking their pose using a single RGB camera, based on prior shape knowledge. The proposed method uses twist-coordinates for pose parametrization and a pixel-wise second-order optimization approach which lead to major improvements in terms of tracking robustness, especially in cases of fast motion and scale changes, compared to previous region-based approaches. Our implementation runs at about 50–100 Hz on a commodity laptop when tracking a single object without relying on GPGPU computations. We compare our method to the current state of the art in various experiments involving challenging motion sequences and diff…

Monocularbusiness.industryComputer scienceComputingMethodologies_IMAGEPROCESSINGANDCOMPUTERVISION020207 software engineering02 engineering and technologyRobustness (computer science)0202 electrical engineering electronic engineering information engineeringRGB color model020201 artificial intelligence & image processingComputer visionSegmentationArtificial intelligenceGeneral-purpose computing on graphics processing unitsbusinessPose
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