Search results for "Protein Subunit"

showing 10 items of 243 documents

Glomerular basement membrane: evidence for collagenous domain of the alpha 3 and alpha 4 chains of collagen IV.

1990

Abstract A collagenous component(s) of Mr = 60K was extracted from glomerular basement membrane with urea and was purified. Upon digestion, it yielded a collagenase-resistant fragment(s) of Mr = 23.5K. Both component and fragment showed immunochemical identity with the noncollagenous domains of the new α3 & α4 chains of collagen IV. The component is characterized by a collagenous domain of about 280 residues and a noncollagenous domain of about 250 residues. These findings further establish these new chains as distinct entities of collagen IV.

Basement membraneGel electrophoresischemistry.chemical_classificationChemistryRenal glomerulusMacromolecular SubstancesProtein ConformationProtein subunitGlomerular basement membraneKidney GlomerulusBiophysicsBiological membraneCell BiologyBiochemistryBasement Membranemedicine.anatomical_structureBiochemistryDomain (ring theory)medicineAnimalsCattleCollagenAmino AcidsGlycoproteinMolecular BiologyBiochemical and biophysical research communications
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Molecular and Functional Characterisation of Hemocyanin of the Giant African Millipede Archispirostreptus gigas

2013

SummaryIn contrast to other terrestrial arthropods where gaseous O2 that fuels aerobic metabolism diffuses to the tissues in tracheal tubes, and most other metazoans where O2 is transported to tissues by circulating respiratory proteins, the myriapods (millipedes and centipedes) strikingly have tracheal systems as well as circulating hemocyanin (Hc). In order to elucidate the evolutionary origin and biological significance of millipede Hc we report the molecular structure (subunit composition and amino acid sequence) of multimeric (36-mer) Hc from the forest-floor dwelling giant African millipede Archispirostreptus gigas and its allosteric oxygen binding properties under various physico-che…

Archispirostreptus gigasGlycosylationPhysiologymedicine.medical_treatmentProtein subunitAllosteric regulationMolecular Sequence DataCoenzymesBohr effectCooperativityAquatic ScienceBiologyModels Biologicalchemistry.chemical_compoundAllosteric RegulationmedicineAnimalsBody SizeMolecular BiologyPeptide sequenceArthropodsEcology Evolution Behavior and SystematicsPhylogenyHemocyaninBayes TheoremHydrogen-Ion Concentrationbiology.organism_classificationOxygenchemistryBiochemistryInsect ScienceAfricaHemocyaninsAnimal Science and ZoologyCalciumElectrophoresis Polyacrylamide GelProtein Binding
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The Proteoglycan NG2 Is Complexed with α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors by the PDZ Glutamate Receptor Interactio…

2003

The proteoglycan NG2 is expressed by immature glial cells in the developing and adult central nervous system. Using the COOH-terminal region of NG2 as bait in a yeast two-hybrid screen, we identified the glutamate receptor interaction protein GRIP1, a multi-PDZ domain protein, as an interacting partner. NG2 exhibits a PDZ binding motif at the extreme COOH terminus which binds to the seventh PDZ domain of GRIP1. In addition to the published expression in neurons, GRIP1 is expressed by immature glial cells. GRIP1 is known to bind to the GluRB subunit of the AMPA glutamate receptor expressed by subpopulations of neurons and immature glial cells. In cultures of primary oligodendrocytes, cells c…

Receptor complexbiologyProtein subunitPDZ domainProtein domainGlutamate receptorCell BiologyAMPA receptorTransfectionBiochemistryMolecular biologynervous systemProteoglycanbiology.proteinMolecular BiologyJournal of Biological Chemistry
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A novel pyruvate kinase (PK-S) from boar spermatozoa is localized at the fibrous sheath and the acrosome

2007

Boar spermatozoa contain a novel pyruvate kinase (PK-S) that is tightly bound at the acrosome of the sperm head and at the fibrous sheath in the principal piece of the flagellum, while the midpiece contains a soluble pyruvate kinase (PK). PK-S could not be solubilized by detergents, but by trypsin with no loss of activity. Purified PK-S as well as PK-S still bound to cell structures and soluble sperm PK have all kinetics similar to those of rabbit muscle PK-M1. The PK-S subunit had a relative molecular mass of 64 ± 1 × 103(n= 3), i.e. slightly higher than that of PK-M1, and carried an N-terminal extension (NH2-TSEAM-COOH) that is lacking in native PK-M1. Evidence is provided that PK-S is en…

MaleEmbryologyErythrocytesSwineProtein subunitBlotting WesternMolecular Sequence DataPyruvate KinaseBiologyEndocrinologySpecies SpecificitymedicineAnimalsAmino Acid SequenceAcrosomeSequence Homology Amino AcidMolecular massAntibodies MonoclonalObstetrics and GynecologyCell BiologyImmunogold labellingTrypsinSpermatozoaSpermReproductive MedicineBiochemistryPolyclonal antibodiesSperm Tailbiology.proteinElectrophoresis Polyacrylamide GelRabbitsSperm MidpieceAcrosomePyruvate kinasemedicine.drugReproduction
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A human CCT5 gene mutation causing distal neuropathy impairs hexadecamer assembly in an archaeal model

2014

Chaperonins mediate protein folding in a cavity formed by multisubunit rings. The human CCT has eight non-identical subunits and the His147Arg mutation in one subunit, CCT5, causes neuropathy. Knowledge is scarce on the impact of this and other mutations upon the chaperone's structure and functions. To make progress, experimental models must be developed. We used an archaeal mutant homolog and demonstrated that the His147Arg mutant has impaired oligomeric assembly, ATPase activity, and defective protein homeostasis functions. These results establish for the first time that a human chaperonin gene defect can be reproduced and studied at the molecular level with an archaeal homolog. The major…

Models MolecularProtein FoldingProtein ConformationProtein subunitMutantMolecular Sequence Datahuman CCT5 gene mutation molecular dynamics neuropathy archaeal modelSequence alignmentGene mutationBiologyArticleChaperonin03 medical and health sciences0302 clinical medicineProtein structureHumansProtein Interaction Domains and MotifsAmino Acid Sequence030304 developmental biologyGenetics0303 health sciencesMultidisciplinarySettore BIO/16 - Anatomia UmanaArchaeaSettore CHIM/08 - Chimica FarmaceuticaChaperone (protein)Mutationbiology.proteinThermodynamicsProtein foldingProtein MultimerizationSequence Alignment030217 neurology & neurosurgeryChaperonin Containing TCP-1
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Fused Dibenzo[ a , m ]rubicene: A New Bowl-Shaped Subunit of C 70 Containing Two Pentagons

2016

Total synthetic approaches of fullerenes are the holy grail for organic chemistry. So far, the main attempts have focused on the synthesis of the buckminsterfullerene C60. In contrast, access to subunits of the homologue C70 remains challenging. Here, we demonstrate an efficient bottom-up strategy toward a novel bowl-shaped polycyclic aromatic hydrocarbons (PAH) C34 with two pentagons. This PAH represents a subunit for C70 and of other higher fullerenes. The bowl-shaped structure was unambiguously determined by X-ray crystallography. A bowl-to-bowl inversion for a C70 fragment in solution was investigated by dynamic NMR analysis, showing a bowl-to-bowl inversion energy (ΔG(⧧)) of 16.7 kcal …

Fullerene010405 organic chemistryStereochemistryProtein subunitGeneral Chemistry010402 general chemistry01 natural sciencesBiochemistryCatalysis0104 chemical sciencesHigher fullereneschemistry.chemical_compoundColloid and Surface ChemistryBuckminsterfullerenechemistryJournal of the American Chemical Society
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Presenilin is the molecular target of acidic γ-secretase modulators in living cells.

2012

The intramembrane-cleaving protease γ-secretase catalyzes the last step in the generation of toxic amyloid-β (Aβ) peptides and is a principal therapeutic target in Alzheimer's disease. Both preclinical and clinical studies have demonstrated that inhibition of γ-secretase is associated with prohibitive side effects due to suppression of Notch processing and signaling. Potentially safer are γ-secretase modulators (GSMs), which are small molecules that selectively lower generation of the highly amyloidogenic Aβ42 peptides but spare Notch processing. GSMs with nanomolar potency and favorable pharmacological properties have been described, but the molecular mechanism of GSMs remains uncertain an…

CellsProtein subunitDrug Evaluation PreclinicalNotch signaling pathwaylcsh:MedicineCHO CellsBiochemistryModels BiologicalPresenilinInhibitory Concentration 50CricetulusCricetinaeAmyloid precursor proteinAnimalsHumansMolecular Targeted TherapyEnzyme InhibitorsMode of actionlcsh:ScienceBiologyCells CulturedMultidisciplinarybiologyEnzyme ClassesChemistryAnti-Inflammatory Agents Non-SteroidalHEK 293 cellslcsh:RChemical ReactionsPresenilinsProteinsSmall moleculeEnzymesChemistryHEK293 CellsNeurologyBiochemistrybiology.proteinMedicineDementialcsh:QAmyloid Precursor Protein SecretasesAmyloid precursor protein secretaseResearch ArticlePLoS ONE
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Amino acids in the second transmembrane helix of the Lhca4 subunit are important for formation of stable heterodimeric light-harvesting complex LHCI-…

2007

Photosynthetic light-harvesting complexes (LHCs) are assembled from apoproteins (Lhc proteins) and non-covalently attached pigments. Despite a considerable amino acid sequence identity, these proteins differ in their oligomerization behavior. To identify the amino acid residues determining the heterodimerization of Lhca1 and Lhca4 to form LHCI-730, we mutated the poorly conserved second transmembrane helix of the two subunits. Mutated genes were expressed in Escherichia coli and the resultant proteins were refolded in vitro and subsequently analyzed by gel electrophoresis. Replacement of the entire second helix in Lhca4 by the one of Lhca3 abolished heterodimerization, whereas it had no eff…

ChlorophyllModels MolecularMolecular Sequence DataLight-Harvesting Protein ComplexesBiologyProtein Structure SecondarySerineSolanum lycopersicumStructural BiologyChlorophyll bindingConsensus sequenceHistidineHomology modelingAmino Acid SequenceAmino AcidsProtein Structure QuaternaryMolecular BiologyPeptide sequenceHistidinePlant Proteinschemistry.chemical_classificationPhotosystem I Protein ComplexAmino acidTransmembrane domainProtein SubunitschemistryBiochemistryMutagenesisChlorophyll Binding ProteinsDimerizationSequence AlignmentJournal of molecular biology
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2015

Elongator is a conserved protein complex comprising six different polypeptides that has been ascribed a wide range of functions, but which is now known to be required for modification of uridine residues in the wobble position of a subset of tRNAs in yeast, plants, worms and mammals. In previous work, we showed that Elongator's largest subunit (Elp1; also known as Iki3) was phosphorylated and implicated the yeast casein kinase I Hrr25 in Elongator function. Here we report identification of nine in vivo phosphorylation sites within Elp1 and show that four of these, clustered close to the Elp1 C-terminus and adjacent to a region that binds tRNA, are important for Elongator's tRNA modification…

Cancer ResearchTRNA modificationProtein subunitSaccharomyces cerevisiaeWobble base pairBiologybiology.organism_classificationBiochemistryCasein Kinase ITransfer RNAGeneticsPhosphorylationProtein kinase AMolecular BiologyGenetics (clinical)Ecology Evolution Behavior and SystematicsPLOS Genetics
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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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