Search results for "FS"

showing 10 items of 1992 documents

High affinity agonistic metal ion binding sites within the melanocortin 4 receptor illustrate conformational change of transmembrane region 3.

2003

We created a molecular model of the human melanocortin 4 receptor (MC4R) and introduced a series of His residues into the receptor protein to form metal ion binding sites. We were able to insert micromolar affinity binding sites for zinc between transmembrane region (TM) 2 and TM3 where the metal ion alone was able to activate this peptide binding G-protein-coupled receptor. The exact conformation of the metal ion interactions allowed us to predict the orientation of the helices, and remodeling of the receptor protein indicated that Glu100 and Ile104 in TM2 and Asp122 and Ile125 in TM3 are directed toward a putative area of activation of the receptor. The molecular model suggests that a rot…

Protein ConformationAmino Acid MotifsPeptide bindingPlasma protein bindingTransfectionBiochemistryCell LineReceptors G-Protein-CoupledProtein structureCyclic AMPHumansPoint MutationBinding siteReceptorMolecular BiologyBinding SitesChemistryMembrane ProteinsCell BiologyMelanocortin 4 receptorCytosolic partZincBiochemistryBiophysicsReceptor Melanocortin Type 4MelanocortinProtein BindingThe Journal of biological chemistry
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Insights into functional aspects of centrins from the structure of N-terminally extended mouse centrin 1

2006

AbstractCentrins are members of the family of Ca2+-binding EF-hand proteins. In photoreceptor cells, centrin isoform 1 is specifically localized in the non-motile cilium. This connecting cilium links the light-sensitive outer segment with the biosynthetic active inner segment of the photoreceptor cell. All intracellular exchanges between these compartments have to occur through this cilium. Three-dimensional structures of centrins from diverse organisms are known, showing that the EF-hand motifs of the N-terminal domains adopt closed conformations, while the C-terminal EF-hand motifs have open conformations. The crystal structure of an N-terminally extended mouse centrin 1 (MmCen1-L) resemb…

Protein ConformationAmino Acid MotifsSequence HomologyPlasma protein bindingEF-handTroponin CMiceStructure-Activity RelationshipProtein structureCalcium-binding proteinConnecting ciliumCentrinAnimalsHumansPhotoreceptor CellsCiliaEF Hand MotifsProtein Structure QuaternaryChemistryEF handCiliumCalcium-Binding ProteinsTerminal Repeat SequencesCalcium-binding proteinSensory SystemsProtein Structure TertiaryCell biologyOphthalmologyCentrinCalciumTransducinsense organsX-ray structureProtein BindingVision Research
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Activation of the p75 neurotrophin receptor through conformational rearrangement of disulphide-linked receptor dimers.

2009

Ligand-mediated dimerization has emerged as a universal mechanism of growth factor receptor activation. Recent structural studies have shown that neurotrophins interact with dimers of the p75 neurotrophin receptor (p75NTR), but the actual mechanism of receptor activation has remained elusive. Here we show that p75NTR forms disulphide-linked dimers independently of neurotrophin binding through the highly conserved Cys257 in its transmembrane domain. Mutation of Cys257 abolished neurotrophin-dependent receptor activity but did not affect downstream signaling by the p75NTR/NgR/Lingo-1 complex in response to MAG, indicating the existence of distinct, ligand-specific activation mechanisms for p7…

Protein ConformationMutantNeuronesReceptor Nerve Growth FactorMiceProtein structureChlorocebus aethiopsNerve Growth FactorLow-affinity nerve growth factor receptorRNA Small InterferingReceptorskin and connective tissue diseasesReceptors neuralsCells CulturedNeuronsCell DeathGeneral NeuroscienceNF-kappa BCell biologyTransmembrane domainSIGNALINGOligopeptidesNeurotrophinProtein BindingSignal Transductionmusculoskeletal diseasesPROTEINSNeuroscience(all)Green Fluorescent ProteinsNerve Tissue ProteinsReceptors Nerve Growth FactorSuperior Cervical GanglionBiologyTransfectionMOLNEUROArticleGrowth factor receptorAnimalsHumansProtein Interaction Domains and MotifsReceptors Growth FactorCysteineBinding SitesMembrane Proteinsbiological factorsRatsnervous systemAnimals NewbornNeurotrophin bindingMutationbiology.proteinsense organsProtein MultimerizationrhoA GTP-Binding ProteinProteïnesNeuron
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The protease domain of procollagen C-proteinase (BMP1) lacks substrate selectivity, which is conferred by non-proteolytic domains.

2007

Abstract Procollagen C-proteinase (PCP) removes the C-terminal pro-peptides of procollagens and also processes other matrix proteins. The major splice form of the PCP is termed BMP1 (bone morphogenetic protein 1). Active BMP1 is composed of an astacin-like protease domain, three CUB (complement, sea urchin Uegf, BMP1) domains and one EGF-like domain. Here we compare the recombinant human full-length BMP1 with its isolated proteolytic domain to further unravel the functional influence of the CUB and EGF domains. We show that the protease domain alone cleaves truncated procollagen VII within the short telopeptide region into fragments of similar size as the full-length enzyme does. However, u…

Protein FoldingCollagen Type VIIDNA Complementarymedicine.medical_treatmentClinical BiochemistryAmino Acid MotifsGene ExpressionGlutamic AcidBiochemistryBone morphogenetic protein 1Mass SpectrometryBone Morphogenetic Protein 1Cell LineSubstrate SpecificityProtein structuremedicineEscherichia coliAnimalsHumansCysteineDisulfidesMolecular BiologyInclusion BodiesMetalloproteinaseProteasebiologyChemistryMetalloendopeptidasesRecombinant ProteinsProtein Structure TertiaryFibronectinProcollagen peptidaseDrosophila melanogasterBiochemistryBone Morphogenetic ProteinsMutationbiology.proteinProtein foldingAstacinBiological chemistry
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Influence of hydrophobic matching on association of model transmembrane fragments containing a minimised glycophorin A dimerisation motif

2005

AbstractThe principles that govern the folding and packing of membrane proteins are still not completely understood. In the present work, we have revisited the glycophorin A (GpA) dimerisation motif that mediates transmembrane (TM) helix association, one of the best-suited models of membrane protein oligomerisation. By using artificial polyleucine TM segments we have demonstrated in this study that a pattern of only five amino acids (GVxxGVxxT) promotes specific dimerisation. Further, we have used this minimised GpA motif to assess the influence of hydrophobic matching on the TM helix packing process in detergent micelles and found that this factor modulates helix–helix association and/or d…

Protein FoldingRecombinant Fusion ProteinsAmino Acid MotifsMolecular Sequence DataBiophysicsBiochemistryMicelleHydrophobic mismatchHydrophobic mismatchStructural BiologyLeucineHelix packingGeneticsGlycophorinAnimalsHumansAmino Acid SequenceGlycophorinsMolecular BiologyPolyacrylamide gel electrophoresischemistry.chemical_classificationbiologyChemistryGlycophorin AProteïnes de membranaMembrane ProteinsMembrane protein associationCell BiologyTransmembrane proteinAmino acidTransmembrane domainBiochemistryMembrane proteinMutationTransmembrane helixBiophysicsbiology.proteinPeptidesDimerizationHydrophobic and Hydrophilic Interactions
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Identification of new claudin family members by a novel PSI-BLAST based approach with enhanced specificity.

2006

In an attempt to develop a novel strategy for the identification of new members of protein families by in silico approaches, we have developed a semi-automated procedure of consecutive PSI-BLAST (Position-Specific-Iterated Basic Local Alignment Search Tool) searches incorporating identificiation as well as subsequent validation of putative candidates. For a proof of concept study we chose the search for novel members of the claudin family. The initial step was an iterated PSI-BLAST search starting with the PMP22_Claudin domain of each known member of the claudin family against the human part of the RefSeq Database. Putative new claudin domains derived from the converged list were evaluated …

Protein familyIn silicoMolecular Sequence DataSequence alignmentBiologycomputer.software_genreBiochemistrySet (abstract data type)Protein structureStructural BiologySequence Analysis ProteinRefSeqFalse positive paradoxHumansAmino Acid SequenceClaudinDatabases ProteinMolecular BiologyPhylogenyReverse Transcriptase Polymerase Chain ReactionComputational BiologyMembrane ProteinsProtein Structure TertiaryData miningcomputerSequence AlignmentProteins
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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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According to the CPLL proteome sheriffs, not all aperitifs are created equal!

2014

Combinatorial peptide ligand libraries (CPLLs) have been adopted for investigating the proteome of a popular aperitif in Northern Italy, called "Amaro Branzi", stated to be an infusion of a secret herbal mixture, of which some ingredients are declared on the label, namely Angelica officinalis, Gentiana lutea and orange peel, sweetened by a final addition of honey. In order to assess the genuineness of this commercial liqueur, we have prepared extracts of the three vegetable ingredients, assessed their proteomes, and compared them to the one found in the aperitif. The amaro's proteome was identified via prior capture with CPLLs at two different pH values (2.2 and 4.8). Via mass spectrometry …

ProteomeGenomic dataBiophysicsOrange (colour)BiochemistryAnalytical ChemistryGentiana luteaPeptide LibraryHumansGentianaAngelica officinalis; Aperitifs; Combinatorial peptide ligand libraries; Gentiana lutea; Low abundance proteome; Mass spectrometry; Alcoholic Beverages; Angelica; Citrus sinensis; Fruit; Gentiana; Honey; Humans; Hydrogen-Ion Concentration; Mass Spectrometry; Peptide Library; Plant Extracts; Plant Proteins; Proteome; Biochemistry; Biophysics; Analytical Chemistry; Molecular BiologyLow abundance proteomeMolecular BiologyAngelicaPlant ProteinsChromatographybiologyMass spectrometryPlant ExtractsAlcoholic BeveragesHoneyHydrogen-Ion Concentrationbiology.organism_classificationNorthern italyAperitifsFruitOfficinalisProteomeAngelica officinalisGentiana luteaCombinatorial peptide ligand librariesCitrus × sinensisGentianaCitrus sinensis
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Identification of enolase as a plasminogen-binding protein in excretory-secretory products ofFasciola hepatica

2004

AbstractWe have followed a combined proteomic approach to identify proteins of Fasciola hepatica that could be involved in host–parasite interactions. Using two-dimensional gel electrophoresis, far Western immunoblot and mass spectrometry analyses, we have identified the enolase enzyme, present in the excretory/secretory materials of F. hepatica, as a human plasminogen-binding protein. This enzyme has an apparent molecular weight of 47 kDa with pI ranging from 6.2 to 7.2. These results suggest that enolase could act as a plasminogen receptor.

ProteomicsAmino Acid MotifsBlotting WesternMolecular Sequence DataEnolaseEnolaseBiophysicsProteomicsBiochemistryMass SpectrometryHost-Parasite InteractionsStructural BiologyHepaticaparasitic diseasesGeneticsAnimalsFasciola hepaticaElectrophoresis Gel Two-DimensionalAmino Acid SequenceIsoelectric PointPlasminogen bindingMolecular BiologyConserved Sequencechemistry.chemical_classificationGel electrophoresisSheepbiologyExcretory–secretoryPlasminogenHelminth ProteinsCell BiologyFasciola hepaticaHydrogen-Ion Concentrationbiology.organism_classificationMolecular biologyMolecular WeightBlotEnzymeLiverchemistryBiochemistryExcretory systemAntigens HelminthPhosphopyruvate HydrataseCarrier ProteinsFEBS Letters
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Psychometric Evaluation of the Basic Psychological Need Satisfaction and Frustration Scale (BPNSFS) in Italy

2017

The purpose of this multistudy report was to adapt the Basic Psychological Need Satisfaction and Frustration Scale (BPNSFS) to the Italian context. Two studies were conducted. In Study 1, we investigated the dimensionality, reliability, and convergent and discriminant validity of the instrument in a sample of 544 participants (males = 41%) from 16 to 35 years old. In Study 2, we replicated the results concerning dimensionality in an independent sample of 502 participants (males = 42%) from 16 to 35 years old. Furthermore, we analyzed measurement invariance across gender. Results of both studies showed that comparing a series of competitive factorial models, the 6-factor model had the best f…

Psychometricsmedia_common.quotation_subjectself-determination theoryApplied psychologyFrustration050109 social psychologyContext (language use)Test validity050105 experimental psychologyEducationLikert scaleSettore M-PSI/04 - Psicologia Dello Sviluppo E Psicologia Dell'EducazioneDevelopmental and Educational Psychologymedicine0501 psychology and cognitive sciencesApplied PsychologySelf-determination theorymedia_common05 social sciencesSettore M-PSI/03 - Psicometriapsychometric evaluationBPNSFSNeed satisfaction need frustration self-determination theory psychometric evaluation BPNSFSneed frustrationScale (social sciences)AnxietyPsychology (miscellaneous)medicine.symptomPsychologyNeed satisfaction
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