Search results for "Transmembrane"

showing 10 items of 299 documents

Identification of two novel polymorphisms and a rare deletion variant in the human dopamine D4 receptor gene

1995

We report two novel polymorphisms and a rare deletion variant in the human dopaine D4 receptor gene. The two polymorphisms are characterized by single base pair substitutions, namely a G-->C transversion changing codon 11 from GGG (encoding Gly) to CGG (encoding Arg) and a C-->T transition in position -11 upstream from the start codon. The Arg11 variant occurs at a frequency of about 1% and the C-->T transition at a frequency of about 7% in German control subjects (n = 148). Allele frequencies observed in patients suffering from schizophrenia (n = 256) and bipolar affective disorder (n = 99) were similar. The deletion variant is characterized by a 21 bp deletion affecting codons 36 to 42 co…

AdultObsessive-Compulsive DisorderBipolar DisorderMolecular Sequence DataBiologymedicine.disease_causePolymerase Chain ReactionGene FrequencyStart codonReference ValuesLeukocytesGeneticsmedicineHumansPoint MutationAmino Acid SequenceAge of OnsetCodonTransversionGeneAllele frequencyBiological PsychiatryGenetics (clinical)DNA PrimersRepetitive Sequences Nucleic AcidSequence DeletionGeneticsMutationBase SequenceTransition (genetics)Receptors Dopamine D2Receptors Dopamine D4Genetic VariationDNAExonsMiddle Agedmedicine.diseasePsychiatry and Mental healthTransmembrane domainSchizophreniaSchizophreniaPanic DisorderPolymorphism Restriction Fragment Length
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Differential cysteine depletion in respiratory chain complexes enables the distinction of longevity from aerobicity.

2010

Mitochondrially encoded proteins in long-lived animals exhibit a characteristic anomaly on the amino acid usage level: they abstain from the use of cysteine in a lifespan-dependent fashion. Here, we have further investigated this phenomenon by analyzing respiratory chain complex subunits individually. We find that complex I cysteine depletion is the almost exclusive carrier of the cysteine-lifespan correlation, whereas complex IV cysteine depletion is uniform in all aerobic animals, unrelated to longevity, but even more pronounced than complex I cysteine depletion in the longest-lived species. In nuclear encoded subunits of the respiratory chain, we find lifespan-independent cysteine deplet…

AgingTime FactorsProtein ConformationRespiratory chainBiologyProtein oxidationProtein Structure SecondaryElectron TransportProtein structureOxygen ConsumptionAnimalsHumansCysteineSulfhydryl CompoundsPhylogenychemistry.chemical_classificationCell NucleusRespiratory chain complexMembrane ProteinsAerobiosisAmino acidMitochondriaProtein Structure TertiaryTransmembrane domainOxidative StressBiochemistrychemistryMembrane proteinDevelopmental BiologyCysteineMechanisms of ageing and development
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Structural Mechanism of N-Methyl-D-Aspartate Receptor Type 1 Partial Agonism

2012

N-methyl-D-aspartate (NMDA) receptors belong to a family of ionotropic glutamate receptors that contribute to the signal transmission in the central nervous system. NMDA receptors are heterotetramers that usually consist of two GluN1 and GluN2 monomers. The extracellular ligand-binding domain (LBD) of a monomer is comprised of discontinuous segments that form the functional domains D1 and D2. While the binding of a full agonist glycine to LBD of GluN1 is linked to cleft closure and subsequent ion-channel opening, partial agonists are known to activate the receptor only sub-maximally. Although the crystal structures of the LBD of related GluA2 receptor explain the mechanism for the partial a…

AgonistProtein Structuremedicine.drug_classGlycineMolecular ConformationBiophysicslcsh:MedicineMolecular Dynamics SimulationLigandsta3111Receptors N-Methyl-D-AspartateBiochemistryBiophysics Simulationsta3112Partial agonistIon ChannelsChemical BiologyMacromolecular Structure AnalysismedicineBiomacromolecule-Ligand Interactionslcsh:ScienceReceptorBiologyta116Ion channelCrystallographyMultidisciplinaryChemistrylcsh:Rta1182Glutamate receptorProteinsComputational BiologyNeurotransmittersProtein Structure TertiaryTransmembrane ProteinsBiochemistryCycloserineBiophysicsNMDA receptorLigand-gated ion channellcsh:Qhormones hormone substitutes and hormone antagonistsProtein BindingResearch ArticleNeuroscienceIonotropic effectPLoS ONE
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Assessment of determinants affecting the dual topology of hepadnaviral large envelope proteins

2004

For functional diversity, the large (L) envelope protein of hepatitis B virus (HBV) acquires a dual transmembrane topology via co-translational membrane integration of the S region and partial post-translational translocation of the preS subdomain. Because each process requires the second transmembrane segment (TM2), we explored the action of this determinant by using protease protection analysis of mutant L proteins. We demonstrated that neither the disruption of a leucine zipper-like motif by multiple alanine substitutions nor the flanking charges of TM2 affected the topological reorientation of L. The dispensability of both putative subunit interaction modules argues against a link betwe…

AlanineHepatitis B virusHepatitis B virusVirus AssemblyAmino Acid MotifsMolecular Sequence DataProtein domainPhenotype mixingBiological TransportBiologyEndoplasmic Reticulummedicine.disease_causeVirologyTransmembrane domainDual topologyAmino Acid SubstitutionViral Envelope ProteinsVirologyMembrane topologymedicineHepadnavirusAmino Acid SequenceProtein Processing Post-TranslationalJournal of General Virology
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Dissection of the relative contribution of the Schizosaccharomyces pombe Ctr4 and Ctr5 proteins to the copper transport and cell surface delivery fun…

2011

The Ctr1 family of proteins mediates high-affinity copper (Cu) acquisition in eukaryotic organisms. In the fission yeastSchizosaccharomyces pombe, Cu uptake is carried out by a heteromeric complex formed by the Ctr4 and Ctr5 proteins. Unlike human andSaccharomyces cerevisiaeCtr1 proteins, Ctr4 and Ctr5 are unable to function independently in Cu acquisition. Instead, both proteins physically interact with each other to form a Ctr4–Ctr5 heteromeric complex, and are interdependent for secretion to the plasma membrane and Cu transport activity. In this study, we usedS. cerevisiaemutants that are defective in high-affinity Cu uptake to dissect the relative contribution of Ctr4 and Ctr5 to the Cu…

Amino Acid MotifsMutantSaccharomyces cerevisiaeSaccharomyces cerevisiaeBiologyMicrobiologySchizosaccharomycesHumansSecretionAmino Acid SequenceSLC31 ProteinsCation Transport ProteinsCell MembraneGenetic Complementation Testbiology.organism_classificationFusion proteinYeastProtein Structure TertiaryCell biologyComplementationTransmembrane domainBiochemistryCell and Molecular Biology of MicrobesSchizosaccharomyces pombeSchizosaccharomyces pombe ProteinsSequence AlignmentCopper
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The transmembrane receptor Uncoordinated5 (Unc5) is essential for heart lumen formation in Drosophila melanogaster

2011

AbstractTransport of liquids or gases in biological tubes is fundamental for many physiological processes. Our knowledge on how tubular organs are formed during organogenesis and tissue remodeling has increased dramatically during the last decade. Studies on different animal systems have helped to unravel some of the molecular mechanisms underlying tubulogenesis. Tube architecture varies dramatically in different organs and different species, ranging from tubes formed by several cells constituting the cross section, tubes formed by single cells wrapping an internal luminal space or tubes that are formed within a cell. Some tubes display branching whereas others remain linear without interse…

AngiogenesisLumen (anatomy)Receptors Cell SurfaceOrganogenesisLumen formationBiologyLigandsUnc5AnimalsDrosophila ProteinsDrosophila heart morphogenesisMyocytes CardiacNerve Growth FactorsReceptorMolecular BiologyCardiogenesisTumor Suppressor ProteinsHeartCell BiologyAnatomyNetrin-1Tubulogenesisbiology.organism_classificationTransmembrane proteinCell biologyDrosophila melanogasterNetrinBSignal transductionDrosophila melanogasterNetrin ReceptorsDrosophila ProteinDevelopmental BiologyDevelopmental Biology
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Sterically geared tris-thioureas; transmembrane chloride transporters with unusual activity and accessibility

2015

Tris-N-arylthioureas derived in one step from 1,3,5-tris(aminomethyl)-2,4,6-triethylbenzene are remarkably effective anion carriers. With optimised aryl substituents their activities come close to the best currently known, suggesting that they might find use as readily available standards in anion transport research.

AnionsModels MolecularTrisSteric effectsCrystallography X-RayChlorideCatalysisPhysico-chimie généralechemistry.chemical_compoundChloridesMaterials ChemistrymedicineChimieMoleculeOrganic chemistryta116Ion transporterIon TransportMolecular StructureChemistryArylThioureatransmembrane anion carriersMetals and Alloystransmembrane transportersGeneral ChemistryCombinatorial chemistryTransmembrane proteinSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsChimie organiqueThioureaCeramics and Compositesmedicine.drugChemical Communications
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Facilitated Anion Transport Induces Hyperpolarization of the Cell Membrane That Triggers Differentiation and Cell Death in Cancer Stem Cells

2015

Facilitated anion transport potentially represents a powerful tool to modulate various cellular functions. However, research into the biological effects of small molecule anionophores is still at an early stage. Here we have used two potent anionophore molecules inspired in the structure of marine metabolites tambjamines to gain insight into the effect induced by these compounds at the cellular level. We show how active anionophores, capable of facilitating the transmembrane transport of chloride and bicarbonate in model phospholipid liposomes, induce acidification of the cytosol and hyperpolarization of plasma cell membranes. We demonstrate how this combined effect can be used against canc…

AnionsPHPhysiologyCellular differentiationTRANSMEMBRANE TRANSPORTChemistry OrganicFisiologiaPROGRESSIONApoptosisNanotechnologyStem cellsBiochemistryCatalysisCell LineMembrane PotentialsCell membraneColloid and Surface ChemistryCancer stem cellBINDINGPathologymedicineHumansSYNTHETIC ION CHANNELSMembrane potentialIon TransportANALOGSChemistryCHLORIDE TRANSPORTCell MembraneApoptosiQuímica orgánicaCell DifferentiationMICROBIOLOGIAGeneral ChemistryHyperpolarization (biology)Membrane transportCARRIERSPatologiaAPOPTOSISCell biologyCytosolmedicine.anatomical_structureLiposomesCancer cellNeoplastic Stem CellsCèl·lules mareJournal of the American Chemical Society
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Interaction of theEscherichia colitransporter DctA with the sensor kinase DcuS: presence of functional DctA/DcuS sensor units

2012

The aerobic Escherichia coli C(4) -dicarboxylate transporter DctA and the anaerobic fumarate/succinate antiporter DcuB function as obligate co-sensors of the fumarate responsive sensor kinase DcuS under aerobic or anaerobic conditions respectively. Overproduction under anaerobic conditions allowed DctA to replace DcuB in co-sensing, indicating their functional equivalence in this capacity. In vivo interaction studies between DctA and DcuS using FRET or a bacterial two-hybrid system (BACTH) demonstrated their interaction. DctA-YFP bound to an affinity column and was able to retain DcuS. DctA shows substantial sequence and secondary structure conservation to Glt(Ph), the Na(+)/glutamate sympo…

AntiporterPlasma protein bindingBiologybiology.organism_classificationmedicine.disease_causeMicrobiologyPyrococcus horikoshiiTransmembrane domainBiochemistryHelixSymportermedicineMolecular BiologyEscherichia coliProtein secondary structureMolecular Microbiology
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Full and Partial Agonism of Ionotropic Glutamate Receptors Indicated by Molecular Dynamics Simulations

2011

Ionotropic glutamate receptors (iGluRs) are synaptic proteins that facilitate signal transmission in the central nervous system. Extracellular iGluR cleft closure is linked to receptor activation; however, the mechanism underlying partial agonism is not entirely understood. Full agonists close the bilobed ligand-binding domain (LBD), while antagonists prevent closure; the transmembrane ion channel either opens or stays closed, respectively. Although some bulky partial agonists produce intermediate iGluR-LBD closure, the available crystal structures also imply that the cleft can be shut with certain partial agonists. Recently, we have shown that the iGluR-LBD closure stage can be recreated b…

Binding SitesProtein ConformationStereochemistryChemistryGeneral Chemical EngineeringGlutamate receptorHydrogen BondingGeneral ChemistryMolecular Dynamics SimulationLibrary and Information SciencesNeurotransmissionCrystallography X-RayLigandsReceptors Ionotropic GlutamateLigand (biochemistry)Partial agonistTransmembrane proteinComputer Science ApplicationsBiophysicsReceptorIon channelProtein BindingIonotropic effectJournal of Chemical Information and Modeling
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