Search results for "Protein topology"

showing 6 items of 6 documents

The SARS-CoV-2 envelope (E) protein has evolved towards membrane topology robustness.

2021

- Single-spanning SARS-CoV-2 envelope (E) protein topology is a major determinant of protein quaternary structure and function. - Charged residues distribution in E protein sequences from highly pathogenic human coronaviruses (i.e., SARS-CoV, MERS-CoV and SARS-CoV-2) stabilize Ntout-Ctin membrane topology. - E protein sequence could have evolved to ensure a more robust membrane topology from MERS-CoV to SARS-CoV and SARS-CoV-2.

EvolutionvirusesBiophysicsBBA Research Lettermedicine.disease_causeBiochemistryEnvelope proteinCell membraneEvolution Molecular03 medical and health sciencesCoronavirus Envelope ProteinsProtein sequencingmedicineHumansskin and connective tissue diseasesProtein Structure Quaternary030304 developmental biologyCoronavirus0303 health sciencesChemistrySARS-CoV-2030302 biochemistry & molecular biologyfungiCell MembraneRobustness (evolution)virus diseasesCell Biologyrespiratory tract diseasesCoronavirusmedicine.anatomical_structureMembrane topologyMembrane topologyBiophysicsProtein quaternary structureProtein topologyFunction (biology)Biochimica et biophysica acta. Biomembranes
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Viral membrane protein topology is dictated by multiple determinants in its sequence.

2009

The targeting, insertion, and topology of membrane proteins have been extensively studied in both prokaryotes and eukaryotes. However, the mechanisms used by viral membrane proteins to generate the correct topology within cellular membranes are less well understood. Here, the effect of flanking charges and the hydrophobicity of the N-terminal hydrophobic segment on viral membrane protein topogenesis are examined systematically. Experimental data reveal that the classical topological determinants have only a minor effect on the overall topology of p9, a plant viral movement protein. Since only a few individual sequence alterations cause an inversion of p9 topology, its topological stability …

GlycosylationViral proteinProtein ConformationMolecular Sequence DataMembrane ProteinsComputational biologyBiologyViral membranemedicine.disease_causeTransloconViral ProteinsProtein structureBiochemistryMembrane proteinStructural BiologyMembrane topologymedicineAmino Acid SequenceProtein topologyMolecular BiologyTopology (chemistry)Journal of molecular biology
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Membrane insertion and topology of the p7B movement protein of Melon Necrotic Spot Virus (MNSV)

2007

AbstractCell-to-cell movement of the Melon Necrotic Spot Virus (MNSV) is controlled by two small proteins working in trans, an RNA-binding protein (p7A) and an integral membrane protein (p7B) separated by an amber stop codon. p7B contains a single hydrophobic region. Membrane integration of this region was observed when inserted into model proteins in the presence of microsomal membranes. Furthermore, we explored the topology and targeting mechanisms of full-length p7B. Here we present evidence that p7B integrates in vitro into the ER membrane cotranslationally and with an Nt-cytoplasmic/Ct-luminal orientation. The observed topology was monitored in vivo by fusing GFP to the Ct of p7B, enab…

Green Fluorescent ProteinsPlant virusBiologyTopologyEndoplasmic ReticulumGreen fluorescent proteinViral ProteinsVirologyMovement proteinIntegral membrane proteinMelon necrotic spot virusEndoplasmic reticulumCarmovirusProteïnes de membranaMembrane Proteinsbiology.organism_classificationMembrane integrationMembrane protein topologyVirusPlant Viral Movement ProteinsMovement proteinsCucurbitaceaeMembraneMembrane proteinCarmovirusMNSVVirology
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Chaperone action in the posttranslational topological reorientation of the hepatitis B virus large envelope protein: Implications for translocational…

2003

The large L envelope protein of the hepatitis B virus utilizes a new folding pathway to acquire a dual transmembrane topology in the endoplasmic reticulum (ER). The process involves cotranslational membrane integration and subsequent posttranslational translocation of its preS subdomain into the ER. Here, we demonstrate that the conformational and functional heterogeneity of L depends on the action of molecular chaperones. Using coimmunoprecipitation, we observed specific interactions between L and the cytosolic Hsc70, in conjunction with Hsp40, and between L and the ER-resident BiP in mammalian cells. Complex formation between L and Hsc70 was abolished when preS translocation was artifici…

Protein ConformationImmunoprecipitationHSC70 Heat-Shock Proteinsmacromolecular substancesTopologyProtein structureViral Envelope ProteinsAnimalsHSP70 Heat-Shock ProteinsEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsMultidisciplinarybiologyEndoplasmic reticulumHSC70 Heat-Shock ProteinsBiological SciencesPrecipitin TestsTransport proteinProtein TransportMembrane topologyChaperone (protein)COS Cellsbiology.proteinProtein topologyCarrier ProteinsProtein Processing Post-TranslationalMolecular ChaperonesProceedings of the National Academy of Sciences
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A computer system to perform structure comparison using TOPS representations of protein structure

2001

We describe the design and implementation of a fast topology-based method for protein structure comparison. The approach uses the TOPS topological representation of protein structure, aligning two structures using a common discovered pattern and generating measure of distance derived from an insert score. Heavy use is made of a constraint-based pattern-matching algorithm for TOPS diagrams that we have designed and described elsewhere (Bioinformatics 15(4) (1999) 317). The comparison system is maintained at the European Bioinformatics Institute and is available over the Web at tops.ebi.ac.uk/tops. Users submit a structure description in Protein Data Bank (PDB) format and can compare it with …

Protein structure databaseMeasure (data warehouse)Molecular StructureComputer scienceGeneral Chemical EngineeringProteinsSequence Homologycomputer.file_formatTOPSProtein structure predictioncomputer.software_genreProtein Data BankApplied Microbiology and BiotechnologyPattern Recognition AutomatedArtificial IntelligencePattern matchingData miningProtein topologyRepresentation (mathematics)computerAlgorithmsSoftwareBiotechnology
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SARS-CoV-2 envelope protein topology in eukaryotic membranes

2020

Coronavirus E protein is a small membrane protein found in the virus envelope. Different coronavirus E proteins share striking biochemical and functional similarities, but sequence conservation is limited. In this report, we studied the E protein topology from the new SARS-CoV-2 virus both in microsomal membranes and in mammalian cells. Experimental data reveal that E protein is a single-spanning membrane protein with the N-terminus being translocated across the membrane, while the C-terminus is exposed to the cytoplasmic side (Nt lum /Ct cyt ). The defined membrane protein topology of SARS-CoV-2 E protein may provide a useful framework to understand its interaction with other viral and ho…

virusescoronavirusmedicine.disease_causeViral Envelope Proteinsmembrane insertionPeptide sequencelcsh:QH301-705.5Topology (chemistry)PhylogenyCoronavirusMutationChemistryGeneral NeuroscienceProteïnes de membranaEukaryotavirus diseases129Recombinant ProteinsCell biologysars-cov-2MembraneProtein topologyCoronavirus InfectionsResearch Article1001topologyPneumonia ViralImmunologySequence alignmentBiologyTopologiaVirusGeneral Biochemistry Genetics and Molecular BiologyBetacoronavirusCoronavirus Envelope ProteinsViral envelopeMicrosomesmedicineHumansAmino Acid SequencePandemicsResearchCell MembraneCOVID-1915envelope proteinMembrane proteinlcsh:Biology (General)CytoplasmMutationSequence AlignmentOpen Biology
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