Search results for "transmembrane domain"

showing 10 items of 99 documents

A member of the Tlr family is involved in dsRNA innate immune response in Paracentrotus lividus sea urchin

2015

Abstract The innate immune response involves proteins such as the membrane receptors of the Toll-like family (TLRs), which trigger different intracellular signalling pathways that are dependent on specific stimulating molecules. In sea urchins, TLR proteins are encoded by members of a large multigenic family composed of 60–250 genes in different species. Here, we report a newly identified mRNA sequence encoding a TLR protein (referred to as Pl-Tlr) isolated from Paracentrotus lividus immune cells. The partial protein sequence contained the conserved Toll/IL-1 receptor (TIR) domain, the transmembrane domain and part of the leucine repeats. Phylogenetic analysis of the Pl-Tlr protein was acco…

LipopolysaccharidesEvolutionImmunologySettore BIO/05 - ZoologiaMediterranean sea urchinParacentrotus lividusImmune systemToll-like receptorPhylogeneticsbiology.animalAnimalsRNA MessengerGeneSea urchinPhylogenyRNA Double-StrandedImmune cellToll-like receptorInnate immune systembiologyEcologyToll-Like ReceptorsReceptors Interleukin-1biology.organism_classificationBiological EvolutionImmunity InnateProtein Structure TertiaryUp-RegulationCell biologyTransmembrane domainPoly I-CSea UrchinsGene expressionDevelopmental BiologyDevelopmental & Comparative Immunology
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Enhanced expression of a cloned and sequenced Ciona intestinalis TNFa-like (CiTNFa) gene during the LPS-induced inflammatory response.

2008

A tumor necrosis factor-alpha (TNFalpha)-like gene from Ciona intestinalis (CiTNF alpha-like) body wall challenged with bacterial lipopolysaccharide (LPS) was cloned and sequenced 4 h after LPS inoculation. An open reading frame of 936 bp encoding a propeptide of 312 amino acids (35.4 kDa) displaying a transmembrane domain from positions 7 to 29, a TACE cleavage site, and a mature peptide domain of 185 amino acids (20.9 kDa), was determined with a predicted isoelectric point of 9.4. The phylogenetic tree based on deduced amino acid sequences of invertebrate TNF-like protein and vertebrate TNFs supported the divergence between the ascidian and vertebrate TNF families, whereas D. melanogaster…

LipopolysaccharidesHemocytesHistologyMolecular Sequence DataSettore BIO/05 - ZoologiaGene ExpressionPathology and Forensic MedicineWestern blotGene expressionHemolymphmedicineTNFα . CiTNFα-like . CiTNFα-like expression . Inflammatory response . Pharynx . Hemocytes . Ciona intestinalis (Tunicata)AnimalsCiona intestinalisAmino Acid SequenceCloning MolecularPeptide sequencePhylogenyInflammationchemistry.chemical_classificationBase Sequencebiologymedicine.diagnostic_testTumor Necrosis Factor-alphaCell Biologybiology.organism_classificationMolecular biologyCiona intestinalisAmino acidTransmembrane domainOpen reading framechemistrySequence Alignment
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USH3A transcripts encode clarin-1, a four-transmembrane-domain protein with a possible role in sensory synapses.

2002

Usher syndrome type 3 (USH3) is an autosomal recessive disorder characterised by the association of post-lingual progressive hearing loss, progressive visual loss due to retinitis pigmentosa and variable presence of vestibular dysfunction. Because the previously defined transcripts do not account for all USH3 cases, we performed further analysis and revealed the presence of additional exons embedded in longer human and mouse USH3A transcripts and three novel USH3A mutations. Expression of Ush3a transcripts was localised by whole mount in situ hybridisation to cochlear hair cells and spiral ganglion cells. The full length USH3A transcript encodes clarin-1, a four-transmembrane-domain protein…

MaleUsher syndromeMolecular Sequence DataBiologyPhotoreceptor cellSynapse03 medical and health sciencesExonMice0302 clinical medicineSequence Analysis ProteinRetinitis pigmentosaHair Cells Auditoryotorhinolaryngologic diseasesGeneticsmedicineAnimalsHumansAmino Acid SequenceGenetics (clinical)Spiral ganglionIn Situ HybridizationPhylogeny030304 developmental biology0303 health sciencesGene Expression ProfilingChromosome MappingMembrane ProteinsSequence Analysis DNAmedicine.diseaseCell biologyPedigreeTransmembrane domainmedicine.anatomical_structureMutationSynapsesFemalesense organsHair cellCalcium ChannelsSequence Alignment030217 neurology & neurosurgeryEuropean journal of human genetics : EJHG
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Sensing by the membrane-bound sensor kinase DcuS: exogenous versus endogenous sensing of C(4)-dicarboxylates in bacteria.

2010

Bacteria are able to grow at the expense of both common (succinate, L-malate, fumarate and aspartate) and uncommon (L-tartrate and D-malate) C4-dicarboxylates, which are components of central metabolism. Two types of sensors/regulators responding to the C4-dicarboxylates function in Escherichia coli, Bacillus, Lactobacillus and related bacteria. The first type represents membrane-integral two-component systems, while the second includes cytoplasmic LysR-type transcriptional regulators. The difference in location and substrate specificity allows the exogenous induction of metabolic genes by common C4-dicarboxylates, and endogenous induction by uncommon C4-dicarboxylates. The two-component s…

Microbiology (medical)Dicarboxylic Acid TransportersModels MolecularBacteriaEscherichia coli ProteinsCell MembraneRegulatory siteGene Expression Regulation BacterialBiologyLigand (biochemistry)MicrobiologyTransmembrane domainBiochemistryProtein kinase domainBacterial ProteinsPAS domainExtracellularEscherichia coliDicarboxylic AcidsBinding siteSignal transductionProtein KinasesSignal TransductionFuture microbiology
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Conversion of the Sensor Kinase DcuS to the Fumarate Sensitive State by Interaction of the Bifunctional Transporter DctA at the TM2/PAS

2021

The membrane-bound C4-dicarboxylate (C4DC) sensor kinase DcuS of Escherichia coli typically forms a protein complex with the C4DC transporter DctA. The DctA × DcuS complex is able to respond to C4DCs, whereas DcuS without DctA is in the permanent ON state. In DctA, the C-terminal helix 8b (H8b) serves as the site for interaction with DcuS. Here the interaction site in DcuS and the related structural and functional adaptation in DcuS were determined. The Linker connecting transmembrane helix 2 (TM2) and the cytosolic PASC (Per-ARNT-SIM) domain of DcuS, was identified as the major site for interaction with DctA-H8b by in vivo interaction studies. The Linker is known to convert the piston-type…

Microbiology (medical)QH301-705.5sensor complexsensor kinase DcuSmedicine.disease_causeMicrobiologyArticle03 medical and health scienceschemistry.chemical_compoundVirologymedicinestructural co-regulatorBiology (General)BifunctionalEscherichia coli030304 developmental biology0303 health sciences030306 microbiologyKinaseTransporterInteraction studiesTransmembrane domainchemistrybifunctional transporter DctAHelixBiophysicsLinkerMicroorganisms
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Structure of the Human TRPML2 Ion Channel Extracytosolic/Lumenal Domain.

2019

Summary TRPML2 is the least structurally characterized mammalian transient receptor potential mucolipin ion channel. The TRPML family hallmark is a large extracytosolic/lumenal domain (ELD) between transmembrane helices S1 and S2. We present crystal structures of the tetrameric human TRPML2 ELD at pH 6.5 (2.0 A) and 4.5 (2.95 A), corresponding to the pH values in recycling endosomes and lysosomes. Isothermal titration calorimetry shows Ca2+ binding to the highly acidic central pre-pore loop which is abrogated at low pH, in line with a pH-dependent channel regulation model. Small angle X-ray scattering confirms the ELD dimensions in solution. Changes in pH or Ca2+ concentration do not affect…

Models Molecular0303 health sciencesBinding SitesTRPMLEndosomeChemistrySmall-angle X-ray scatteringProtein Conformation030302 biochemistry & molecular biologyIsothermal titration calorimetryHydrogen-Ion ConcentrationCrystallography X-Ray03 medical and health sciencesTransient receptor potential channelTransmembrane domainTransient Receptor Potential ChannelsProtein DomainsStructural BiologyBiophysicsHumansCalciumMolecular BiologyProtein secondary structureIon channel030304 developmental biologyStructure (London, England : 1993)
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Charge Pair Interactions in Transmembrane Helices and Turn Propensity of the Connecting Sequence Promote Helical Hairpin Insertion

2013

alpha-Helical hairpins, consisting of a pair of closely spaced transmembrane (TM) helices that are connected by a short interfacial turn, are the simplest structural motifs found in multi-spanning membrane proteins. In naturally occurring hairpins, the presence of polar residues is common and predicted to complicate membrane insertion. We postulate that the pre-packing process offsets any energetic cost of allocating polar and charged residues within the hydrophobic environment of biological membranes. Consistent with this idea, we provide here experimental evidence demonstrating that helical hairpin insertion into biological membranes can be driven by electrostatic interactions between clo…

Models MolecularBioquímicaProtein FoldingGlycosylationMolecular Sequence Datamembrane integrationEndoplasmic Reticulumsalt bridgeProtein Structure SecondaryTurn (biochemistry)Viral Proteins03 medical and health sciencesProtein structureStructural BiologyComputer SimulationAmino Acid SequenceAmino AcidsStructural motifMolecular Biologytranslocon030304 developmental biology0303 health sciencesBinding SitesChemistry030302 biochemistry & molecular biologyProteïnes de membranaBiochemistry and Molecular BiologyMembrane ProteinsBiological membraneTransloconelectrostatic interactionsTransmembrane proteinProtein Structure TertiaryPoliovirusProtein TransportCrystallographyTransmembrane domainhelical hairpinMembrane proteinMutationBiophysicsElectrophoresis Polyacrylamide GelHydrophobic and Hydrophilic InteractionsBiokemi och molekylärbiologi
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Plasticity of the PAS domain and a potential role for signal transduction in the histidine kinase DcuS

2008

The mechanistic understanding of how membrane-embedded sensor kinases recognize signals and regulate kinase activity is currently limited. Here we report structure-function relationships of the multidomain membrane sensor kinase DcuS using solid-state NMR, structural modeling and mutagenesis. Experimental data of an individual cytoplasmic Per-Arnt-Sim (PAS) domain were compared to structural models generated in silico. These studies, together with previous NMR work on the periplasmic PAS domain, enabled structural investigations of a membrane-embedded 40-kDa construct by solid-state NMR, comprising both PAS segments and the membrane domain. Structural alterations are largely limited to prot…

Models MolecularCytoplasmHistidine KinaseMolecular Sequence DataHAMP domainStructural BiologyPAS domainEscherichia coliAmino Acid SequenceKinase activityProtein Structure QuaternaryNuclear Magnetic Resonance BiomolecularMolecular BiologybiologyEscherichia coli ProteinsHistidine kinaseProtein Structure TertiaryCell biologyTransmembrane domainBiochemistryProtein kinase domainCyclic nucleotide-binding domainbiology.proteinGRB2Protein KinasesSignal Transduction
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Transmembrane helix–helix interactions are modulated by the sequence context and by lipid bilayer properties

2012

Abstract Folding of polytopic transmembrane proteins involves interactions of individual transmembrane helices, and multiple TM helix–helix interactions need to be controlled and aligned to result in the final TM protein structure. While defined interaction motifs, such as the GxxxG motif, might be critically involved in transmembrane helix–helix interactions, the sequence context as well as lipid bilayer properties significantly modulate the strength of a sequence specific transmembrane helix–helix interaction. Structures of 11 transmembrane helix dimers have been described today, and the influence of the sequence context as well as of the detergent and lipid environment on a sequence spec…

Models MolecularLateral pressureLipid BilayersMolecular Sequence DataBiophysicsModels BiologicalBiochemistryProtein Structure SecondaryProtein structureAmino Acid SequenceLipid bilayerHydrogen bondGxxxGChemistryHydrogen bondMembrane ProteinsHydrophobic thicknessCell BiologyTransmembrane proteinTransmembrane domainCrystallographyMembraneMembrane proteinMembrane proteinBiophysicsProtein foldingHelix dimerProtein BindingBiochimica et Biophysica Acta (BBA) - Biomembranes
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A Ser residue influences the structure and stability of a Pro-kinked transmembrane helix dimer

2012

AbstractWhen localized adjacent to a Pro-kink, Thr and Ser residues can form hydrogen bonds between their polar hydroxyl group and a backbone carbonyl oxygen and thereby modulate the actual bending angle of a distorted transmembrane α-helix. We have used the homo-dimeric transmembrane cytochrome b559′ to analyze the potential role of a highly conserved Ser residue for assembly and stabilization of transmembrane proteins. Mutation of the conserved Ser residue to Ala resulted in altered heme binding properties and in increased stability of the holo-protein, most likely by tolerating subtle structural rearrangements upon heme binding. The results suggest a crucial impact of an intrahelical Ser…

Models MolecularProlineHeme bindingStereochemistryDimerMolecular ConformationBiophysicsCofactor bindingHemeBiochemistryProtein Structure Secondarychemistry.chemical_compoundProtein structureProtein stabilitySerineProtein foldingCofactor bindingHydrogen bondCell MembranePhotosystem II Protein ComplexHydrogen BondingCell BiologyCytochrome b GroupTransmembrane proteinProtein Structure TertiaryOxygenTransmembrane domainHelix interactionchemistrySpectrophotometryMembrane proteinMutationTransmembrane helixProtein foldingDimerizationProtein BindingBiochimica et Biophysica Acta (BBA) - Biomembranes
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