Search results for "Amino Acid Motifs"

showing 10 items of 79 documents

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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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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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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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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The induction of cytochrome P450 3A5 (CYP3A5) in the human liver and intestine is mediated by the xenobiotic sensors pregnane X receptor (PXR) and co…

2004

Induction of cytochrome P450 3A (CYP3A) by xenobiotics may lead to clinically relevant drug interactions. In contrast with other CYP3A family members, studies on the inducibility of CYP3A5 indicate conflicting results. We report the induction of CYP3A5 mRNA in 13 of 16 hepatocyte preparations exposed to rifampin. Furthermore, induction of CYP3A5 mRNA was observed in intestinal biopsies in three of eight probands following exposure to the antibiotic. The highest absolute levels of CYP3A5 transcripts were found following rifampin treatment in hepatocytes and intestines from carriers of CYP3A5*1 alleles. Elucidation of the mechanism involved in CYP3A5 induction revealed that constitutively act…

Receptors SteroidTime FactorsCYP3ABiopsyAmino Acid MotifsReceptors Cytoplasmic and NuclearPharmacology030226 pharmacology & pharmacyBiochemistryTransactivation0302 clinical medicineCytochrome P-450 Enzyme SystemGenes ReporterCytochrome P-450 CYP3AIntestinal MucosaReceptorPromoter Regions GeneticGenes Dominant0303 health sciencesPregnane X receptorPregnane X Receptor3. Good healthmedicine.anatomical_structureLiverHepatocyteRifampinPlasmidsProtein BindingTranscriptional ActivationHeterozygoteGenotypeBiologyTransfectionXenobiotics03 medical and health sciencesmedicineHumansRNA MessengerMolecular BiologyAllelesConstitutive Androstane Receptor030304 developmental biologyMessenger RNACYP3A4Cell BiologyMolecular biologyProtein Structure TertiaryHepatocytesRNADrug metabolismTranscription FactorsThe Journal of biological chemistry
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Flanking regions determine the structure of the poly-glutamine homo- repeat in huntingtin through mechanisms common among glutamine-rich human protei…

2020

International audience; The causative agent of Huntington's disease, the poly-Q homo-repeat in the N-terminal region of huntingtin (httex1), is flanked by a 17-residue-long fragment (N17) and a proline-rich region (PRR), which promote and inhibit the aggregation propensity of the protein, respectively, by poorly understood mechanisms. Based on experimental data obtained from site-specifically labeled NMR samples, we derived an ensemble model of httex1 that identified both flanking regions as opposing poly-Q secondary structure promoters. While N17 triggers helicity through a promiscuous hydrogen bond network involving the side chains of the first glutamines in the poly-Q tract, the PRR prom…

Repetitive Sequences Amino AcidHuntingtinAmino Acid Motifs[SDV.BBM.BP] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biophysics03 medical and health sciencesHuntington's diseaseStructural BiologyHuman proteome projectmedicineHumans[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Molecular BiologyHuman proteinsProtein secondary structure[SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]030304 developmental biology[INFO.INFO-BI] Computer Science [cs]/Bioinformatics [q-bio.QM]Huntingtin Protein0303 health sciencesChemistry030302 biochemistry & molecular biologyPromotermedicine.diseaseCell biologyIntrinsically Disordered ProteinsGlutamine[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsPolyglutamic Acid[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]Low Complexity Region
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Improving baculovirus transduction of mammalian cells by surface display of a RGD-motif

2006

An RGD-containing peptide, comprising 23 amino acids from the foot-and-mouth disease virus (FMDV) VP1 protein was engineered into the envelope of Autographa californica nuclear polyhedrosis virus surface (AcNPV) using two different display strategies. The RGD-motif is a well-described tripeptide, that by binding to cell surface integrins facilitates virus entry into cells. This epitope was displayed, either by directly modifying the native major envelope protein gp64 of AcNPV, or by incorporating a second, modified version of gp64 onto the virus surface. Transduction efficiencies of four mammalian cell lines were compared by detecting the expression of the reporter gene green fluorescent pr…

Reporter genebiologyvirusesAmino Acid MotifsGenetic VectorsBioengineeringGeneral Medicinebiology.organism_classificationApplied Microbiology and BiotechnologyMolecular biologyRecombinant ProteinsVirusEpitopeGreen fluorescent proteinViral ProteinsTransduction (genetics)Autographa californicaTransduction GeneticViral entryAnimalsHumansBaculoviridaeOligopeptidesBiotechnologyRGD motifJournal of Biotechnology
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Zasp/Cypher internal ZM-motif containing fragments are sufficient to co-localize with α-actinin—Analysis of patient mutations

2005

Z-band alternatively spliced PDZ-containing protein (ZASP/Cypher) has an important role in maintaining Z-disc stability in striated and cardiac muscle. ZASP/Cypher interacts through its PDZ domain with the major Z-disc actin cross-linker, alpha-actinin. ZASP/Cypher also has a conserved sequence called the ZM-motif, and it is found in two alternatively spliced exons 4 and 6. We have shown earlier that the ZM-motif containing internal regions of two related proteins ALP and CLP36 interact with alpha-actinin rod region, and that the ZM-motif is important in targeting ALP to the alpha-actinin containing structures in cell. Here, we show that the ZASP/Cypher internal fragments containing either …

SarcomeresAmino Acid MotifsPDZ domainCHO Cellsmacromolecular substancesBiologyConserved sequenceStress fiber assemblyMyoblastsMiceExonCricetinaeStress FibersmedicineAnimalsHumansMyocyteActininMuscle SkeletalActinAdaptor Proteins Signal TransducingOrganellesGeneticsMyocardiumPoint mutationCardiac muscleExonsIntracellular MembranesCell BiologyLIM Domain Proteinsmusculoskeletal systemPeptide FragmentsCell biologymedicine.anatomical_structureMutationCardiomyopathiesProtein BindingExperimental Cell Research
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Nimrod, a Putative Phagocytosis Receptor with EGF Repeats in Drosophila Plasmatocytes

2007

SummaryThe hemocytes, the blood cells of Drosophila, participate in the humoral and cellular immune defense reactions against microbes and parasites [1–8]. The plasmatocytes, one class of hemocytes, are phagocytically active and play an important role in immunity and development by removing microorganisms as well as apoptotic cells. On the surface of circulating and sessile plasmatocytes, we have now identified a protein, Nimrod C1 (NimC1), which is involved in the phagocytosis of bacteria. Suppression of NimC1 expression in plasmatocytes inhibited the phagocytosis of Staphylococcus aureus. Conversely, overexpression of NimC1 in S2 cells stimulated the phagocytosis of both S. aureus and Esc…

Staphylococcus aureusHemocytesMICROBIOEGF-like domainPhagocytosisAmino Acid MotifsReceptors Cell SurfaceBiologymedicine.disease_causeGeneral Biochemistry Genetics and Molecular BiologyPhagocytosisEscherichia colimedicineMelanogasterAnimalsDrosophila ProteinsReceptors ImmunologicReceptorEscherichia coliGeneAgricultural and Biological Sciences(all)Biochemistry Genetics and Molecular Biology(all)Schneider 2 cellsbiology.organism_classificationTransmembrane proteinCell biologyDrosophilaCELLBIOGeneral Agricultural and Biological SciencesCurrent Biology
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