Search results for "Sequence Alignment"

showing 10 items of 447 documents

Crystal structure of bacteriophage fr capsids at 3.5 A resolution.

1994

The structure of recombinant capsids of the bacterial virus fr has been determined by X-ray crystallography at 3.5 A resolution. The capsids were produced by expressing the fr coat protein in Escherichia coli, the natural host of the virus, and are probably essentially identical to the protein shell of the native virus. The structure was determined using molecular replacement with the protein shell of the related MS2 virus, and refined to a crystallographic R-factor of 0.228. A comparison of the protein shells of the viruses shows that they are very similar, and indicates that they may have a similar regulation of the assembly of the quasi-symmetrical protein shell.

Protein ConformationvirusesMolecular Sequence DataRNA PhagesBiologymedicine.disease_causeCrystallography X-RayViruslaw.inventionBacteriophageCapsidStructural BiologylawmedicineComputer GraphicsEscherichia coliMolecular replacementAmino Acid SequenceMolecular BiologyEscherichia coliConserved SequenceLevivirusResolution (electron density)biology.organism_classificationRecombinant ProteinsCrystallographyCapsidMutationBiophysicsRecombinant DNABacterial virusSequence AlignmentJournal of molecular biology
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RNA-binding ability of PIPP in requires the entire protein

2003

Post-transcriptional fate of eukaryotic mRNAs depends on association with different classes of RNA-binding proteins (RBPs). Among these proteins, the cold-shock domain (CSD)-containing proteins, also called Y-box proteins, play a key role in controlling the recruitment of mRNA to the translational machinery, in response to environmental cues, both in development and in differentiated cells. We recently cloned a rat cDNA encoding a new CSD-protein that we called PIPPin. This protein also contains two putative double-stranded RNA-binding motifs (PIP(1) and PIP(2)) flanking the central CSD, and is able to bind mRNAs encoding H1 degrees and H3.3 histone variants. In order to clarify the role of…

Protein FoldingNerve Tissue ProteinsSequence alignmentRNA-binding proteinPlasma protein bindingArticleRNA-binding proteinscold-shock domainPIPPinhistone variantsHistonesSettore BIO/10 - BiochimicaComplementary DNAHistone H2AAnimalsRNA MessengerGeneticsMessenger RNAbiologyRNA-Binding ProteinsRNACell BiologyRecombinant ProteinsProtein Structure TertiaryRatsCell biologyHistoneGene Expression Regulationbiology.proteinMolecular MedicineSequence AlignmentProtein BindingJournal of Cellular and Molecular Medicine
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Calcium negatively regulates meprin β activity and attenuates substrate cleavage

2015

The meprin β metalloproteinase is an important enzyme in extracellular matrix turnover, inflammation, and neurodegeneration in humans and mice. Previous studies showed a diminished cleavage of certain meprin β substrates in the presence of calcium, although the mechanism was not clear. With the help of a specific fluorogenic peptide assay and the human amyloid precursor protein as substrate, we demonstrated that the influence of calcium is most likely a direct effect on human meprin β itself. Analyzing the crystal structures of pro- and mature meprin β helped to identify a cluster of negatively charged amino acids forming a potential calcium binding site. Mutation of 2 of these residues (D2…

Protein Foldingchemistry.chemical_elementCalciumEndoplasmic ReticulumBiochemistryCell LineSubstrate SpecificityAmyloid beta-Protein PrecursorChlorocebus aethiopsGeneticsAmyloid precursor proteinAnimalsHumansAmino Acid SequenceBinding siteProtein precursorMolecular BiologyCellular localizationSecretory pathwayMetalloproteinaseAmyloid beta-PeptidesBinding SitesbiologyEndoplasmic reticulumMetalloendopeptidasesCell biologyHEK293 CellschemistryCOS CellsMutationMetalloproteasesbiology.proteinCalciumAmyloid Precursor Protein SecretasesSequence AlignmentBiotechnologyThe FASEB Journal
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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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Novel avidin-like protein from a root nodule symbiotic bacterium, Bradyrhizobium japonicum.

2005

Bradyrhizobium japonicum is an important nitrogenfixing symbiotic bacterium, which can form root nodules on soybeans. These bacteria have a gene encoding a putative avidin- and streptavidin-like protein, which bears an amino acid sequence identity of only about 30% over the core regions with both of them. We produced this protein in Escherichia coli both as the full-length wild type and as a C-terminally truncated core form and showed that it is indeed a high affinity biotin-binding protein that resembles (strept)avidin structurally and functionally. Because of the considerable dissimilarity in the amino acid sequence, however, it is immunologically very different, and polyclonal rabbit and…

Protein familyProtein ConformationMolecular Sequence DataBiotinmedicine.disease_causeBiochemistryBacterial ProteinsmedicineAnimalsHumansAmino Acid SequenceBradyrhizobiumAntigensMolecular BiologyGeneEscherichia coliPeptide sequencebiologyCell Biologybiology.organism_classificationAvidinBiochemistryPolyclonal antibodiesbiology.proteinRabbitsCarrier ProteinsSequence AlignmentBacteriaBradyrhizobium japonicumAvidinThe Journal of biological chemistry
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Evolution of nacre: biochemistry and proteomics of the shell organic matrix of the cephalopod Nautilus macromphalus.

2009

12 pages; International audience; In mollusks, one of the most widely studied shell textures is nacre, the lustrous aragonitic layer that constitutes the internal components of the shells of several bivalves, a few gastropods, and one cephalopod: the nautilus. Nacre contains a minor organic fraction, which displays a wide range of functions in relation to the biomineralization process. Here, we have biochemically characterized the nacre matrix of the cephalopod Nautilus macromphalus. The acid-soluble matrix contains a mixture of polydisperse and discrete proteins and glycoproteins, which interact with the formation of calcite crystals. In addition, a few bind calcium ions. Furthermore, we h…

ProteomeShell (structure)ProteomicsBiochemistryCalcium Carbonate03 medical and health sciencesPaleontologychemistry.chemical_compoundproteomicsevolutionAnimals14. Life underwaterAmino Acid SequenceNautilus[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular BiologyChromatography High Pressure Liquid030304 developmental biologyCalciteNautilus macromphalus0303 health sciencesbiology030302 biochemistry & molecular biologyOrganic ChemistryProteinsbiology.organism_classificationbiomineralization[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsBiological EvolutionCephalopodCalcium carbonatechemistryChemical engineeringSolubilitySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationMolecular MedicineNautilusNautilus macromphalusSequence AlignmentBiomineralizationmollusk shell nacre
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Phylointeractomics reconstructs functional evolution of protein binding

2017

Molecular phylogenomics investigates evolutionary relationships based on genomic data. However, despite genomic sequence conservation, changes in protein interactions can occur relatively rapidly and may cause strong functional diversification. To investigate such functional evolution, we here combine phylogenomics with interaction proteomics. We develop this concept by investigating the molecular evolution of the shelterin complex, which protects telomeres, across 16 vertebrate species from zebrafish to humans covering 450 million years of evolution. Our phylointeractomics screen discovers previously unknown telomere-associated proteins and reveals how homologous proteins undergo functiona…

Proteomics0301 basic medicineLineage (evolution)ScienceTelomere-Binding ProteinsGeneral Physics and AstronomyGenomicsBiologyProteomicsArticleGeneral Biochemistry Genetics and Molecular BiologyConserved sequenceEvolution Molecular03 medical and health sciencesPhylogeneticsMolecular evolutionPhylogenomicsAnimalsCells CulturedConserved SequencePhylogenyGeneticsGenomeMultidisciplinaryQComputational BiologyGenomicsSequence Analysis DNAGeneral ChemistryTelomereProtein superfamily030104 developmental biologyEvolutionary biologyVertebratesSequence AlignmentProtein Binding
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Large-scale analysis of SARS-CoV-2 spike-glycoprotein mutants demonstrates the need for continuous screening of virus isolates

2021

Due to the widespread of the COVID-19 pandemic, the SARS-CoV-2 genome is evolving in diverse human populations. Several studies already reported different strains and an increase in the mutation rate. Particularly, mutations in SARS-CoV-2 spike-glycoprotein are of great interest as it mediates infection in human and recently approved mRNA vaccines are designed to induce immune responses against it. We analyzed 1,036,030 SARS-CoV-2 genome assemblies and 30,806 NGS datasets from GISAID and European Nucleotide Archive (ENA) focusing on non-synonymous mutations in the spike protein. Only around 2.5% of the samples contained the wild-type spike protein with no variation from the reference. Among…

RNA virusesMutation rateCoronavirusesEpidemiologyMolecular biologyT-LymphocytesMutantGene Identification and Analysismedicine.disease_causeGenomeWhite Blood CellsDatabase and Informatics MethodsSequencing techniquesMutation RateAnimal CellsDNA sequencingPathology and laboratory medicineGeneticsMutationMultidisciplinaryT CellsMicrobial MutationQRHigh-Throughput Nucleotide SequencingGenomicsMedical microbiologyVirusesSpike Glycoprotein CoronavirusMedicineSARS CoV 2PathogensCellular TypesTranscriptome AnalysisSequence AnalysisResearch ArticleNext-Generation SequencingSARS coronavirusBioinformaticsImmune CellsScienceImmunologyProtein domainSequence alignmentGenomicsGenome ViralBiologyMicrobiologyAntibodiesDNA sequencingProtein DomainsGeneticsmedicineHumansMutation DetectionPandemicsMedicine and health sciencesBlood CellsBiology and life sciencesSARS-CoV-2OrganismsViral pathogensComputational BiologyCOVID-19Cell BiologyGenome AnalysisMicrobial pathogensResearch and analysis methodsMolecular biology techniquesMutationSequence AlignmentPLOS ONE
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Development of type-specific and cross-reactive serological probes for the minor capsid protein of human papillomavirus type 33.

1993

Human papillomavirus type 33 (HPV33) is associated with malignant tumors of the cervix. In an attempt to develop immunological probes for HPV33 infections, antisera against various bacterial fusion proteins carrying sequences of the minor capsid protein encoded by L2 were raised in animals. Antigenic determinants on the HPV33 L2 protein were identified by using truncated fusion proteins and were classified as type specific or cross-reactive with respect to HPV1, -8, -11, -16, and -18. Cross-reactive epitopes map to amino acids 98 to 107 or to amino acids 102 to 112 and 107 to 117, respectively, depending on the fusion protein used for immunization. Antibodies directed toward these epitopes …

Recombinant Fusion ProteinsImmunologyGuinea PigsMolecular Sequence DataPeptideBiologyMicrobiologyEpitopeStructure-Activity RelationshipCapsidAntigenSpecies SpecificityVirologyAnimalsAmino Acid SequenceStaphylococcal Protein APeptide sequenceAntigens ViralPapillomaviridaeGlutathione TransferaseSequence Deletionchemistry.chemical_classificationBase SequenceOncogene Proteins Viralbeta-GalactosidaseMolecular biologyFusion proteinAmino acidchemistryCapsidOligodeoxyribonucleotidesInsect Sciencebiology.proteinCapsid ProteinsRabbitsAntibodySequence AlignmentResearch ArticleJournal of virology
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ZFWD: a novel subfamily of plant proteins containing a C3H zinc finger and seven WD40 repeats

2000

We describe a new subfamily of WD repeat proteins characterised by the presence of a C3H zinc finger at the N-terminal part of the protein associated with seven WD40 repeats. We have identified four members of this subfamily in Arabidopsis thaliana, one of them with associated expressed sequence tags (ESTs). We have also identified homologous ESTs in rice, cotton, maize, poplar, pine tree and the ice plant. We do not observe animal homologues, suggesting that this subfamily could be specific for plants. Our data suggest an important role for these proteins. Based on the high sequence conservation within the conserved domains, we suggest that these proteins could have a regulatory function.

Repetitive Sequences Amino AcidDNA ComplementarySubfamilyDNA PlantMolecular Sequence DataArabidopsisSequence alignmentBiologyEvolution MolecularWD40 repeatGeneticsProtein IsoformsArabidopsis thalianaAmino Acid SequencePeptide sequencePhylogenyPlant ProteinsExpressed Sequence TagsGeneticsZinc fingerExpressed sequence tagProtein subfamilySequence Homology Amino AcidArabidopsis Proteinsfungifood and beveragesZinc FingersSequence Analysis DNAGeneral Medicinebiology.organism_classificationSequence AlignmentGene
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