Search results for " glycoprotein"

showing 10 items of 430 documents

Protein Kinase C μ Is Regulated by the Multifunctional Chaperon Protein p32

2000

We identified the multifunctional chaperon protein p32 as a protein kinase C (PKC)-binding protein interacting with PKCalpha, PKCzeta, PKCdelta, and PKC mu. We have analyzed the interaction of PKC mu with p32 in detail, and we show here in vivo association of PKC mu, as revealed from yeast two-hybrid analysis, precipitation assays using glutathione S-transferase fusion proteins, and reciprocal coimmunoprecipitation. In SKW 6.4 cells, PKC mu is constitutively associated with p32 at mitochondrial membranes, evident from colocalization with cytochrome c. p32 interacts with PKC mu in a compartment-specific manner, as it can be coimmunoprecipitated mainly from the particulate and not from the so…

ImmunoprecipitationRecombinant Fusion ProteinsGolgi ApparatusSaccharomyces cerevisiaeSpodopteraMitogen-activated protein kinase kinaseBiologyTransfectionBiochemistryCell LineMitochondrial ProteinsAnimalsHumansCloning MolecularKinase activityMolecular BiologyProtein Kinase CProtein kinase CGlutathione TransferaseB-LymphocytesBinding SitesMembrane GlycoproteinsKinaseAutophosphorylationJNK Mitogen-Activated Protein KinasesCell BiologyFusion proteinMitochondriaReceptors ComplementCell biologybody regionsHyaluronan ReceptorsProtein kinase domainBiochemistryMitogen-Activated Protein KinasesCarrier ProteinsMolecular ChaperonesProtein BindingJournal of Biological Chemistry
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In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges

2020

Flexible spikes The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein enables viral entry into host cells by binding to the angiotensin-converting enzyme 2 (ACE2) receptor and is a major target for neutralizing antibodies. About 20 to 40 spikes decorate the surface of virions. Turoňová et al. now show that the spike is flexibly connected to the viral surface by three hinges that are well protected by glycosylation sites. The flexibility imparted by these hinges may explain how multiple spikes act in concert to engage onto the flat surface of a host cell. Science, this issue p. 203

In situElectron Microscope TomographyGlycanGlycosylationFlexibility (anatomy)virusesProtein domainPneumonia ViralHingeMolecular Dynamics SimulationBiologylaw.inventionBetacoronavirusProtein DomainslawTarget identificationmedicineHumansPandemicsResearch ArticlesHost cell surfaceMultidisciplinarySARS-CoV-2R-ArticlesCryoelectron MicroscopyBiochemCOVID-19MicrobioResearch HighlightCell biologymedicine.anatomical_structureSpike Glycoprotein Coronavirusbiology.proteinRecombinant DNASpike (software development)Protein MultimerizationStructural biologyCoronavirus InfectionsResearch ArticleScience (New York, N.y.)
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MMGBSA As a Tool To Understand the Binding Affinities of Filamin–Peptide Interactions

2013

Filamins (FLN) are large dimeric proteins that cross-link actin and work as important scaffolds in human cells. FLNs consist of an N-terminal actin-binding domain followed by 24 immunoglobulin-like domains (FLN1-24). FLN domains are divided into four subgroups based on their amino acid sequences. One of these subgroups, including domains 4, 9, 12, 17, 19, 21, and 23, shares a similar ligand-binding site between the β strands C and D. Several proteins, such as integrins β2 and β7, glycoprotein Ibα (GPIbα), and migfilin, have been shown to bind to this site. Here, we computationally estimated the binding free energies of filamin A (FLNa) subunits with bound peptides using the molecular mechan…

Integrin beta ChainsFilaminsGeneral Chemical EngineeringIntegrinPeptidePlasma protein bindingMolecular Dynamics SimulationLibrary and Information SciencesBiologyLigandsFilaminta3111Protein Structure SecondaryProtein structureProtein Interaction MappingHumansFLNAProtein Interaction Domains and MotifsBinding siteta116chemistry.chemical_classificationBinding Sitesta1182General ChemistryComputer Science ApplicationsAmino acidCytoskeletal ProteinsCrystallographyPlatelet Glycoprotein GPIb-IX ComplexchemistryCD18 AntigensBiophysicsbiology.proteinThermodynamicsPeptidesCell Adhesion MoleculesAlgorithmsProtein BindingJournal of Chemical Information and Modeling
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On the origin of Metazoan adhesion receptors: cloning of integrin alpha subunit from the sponge Geodia cydonium

1997

Integrins are prominent receptors known from vertebrates and the higher phyla of invertebrates. Until now, no evidence has been provided for the existence of integrins in the lowest Metazoa, the sponges (Porifera). We have isolated and characterized a cDNA clone encoding the alpha subunit of integrin from the marine sponge Geodia cydonium (GCINTEG). The open reading frame encodes a polypeptide of 1,086 residues (118 kDa). The intracellular domain features the sequence Tyr-Phe-x-Gly-Phe-Phe-x-Arg, which is different in one residue from the characteristic consensus pattern for integrin alpha subunits. We conclude that sponges, the oldest multicellular animal phylum, already utilize the struct…

IntegrinsDNA ComplementaryMolecular Sequence DataIntegrinExtracellular matrixGeneticsAnimalsCloning MolecularReceptorMolecular BiologyEcology Evolution Behavior and SystematicsG alpha subunitCloningMembrane GlycoproteinsBase SequenceSequence Homology Amino AcidbiologyMembrane Proteinsbiology.organism_classificationPoriferaCell biologySuberites domunculaOpen reading frameSpongePlatelet Glycoprotein GPIb-IX Complexbiology.proteinMolecular Biology and Evolution
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Dystroglycan in Skin and Cutaneous Cells: β-Subunit Is Shed from the Cell Surface

2004

In skin, hemidesmosomal protein complexes attach the epidermis to the dermis and are critical for stable connection of the basal epithelial cell cytoskeleton with the basement membrane (BM). In muscle, a similar supramolecular aggregate, the dystrophin glycoprotein complex links the inside of muscle cells with the BM. A component of the muscle complex, dystroglycan (DG), also occurs in epithelia. In this study, we characterized the expression and biochemical properties of authentic and recombinant DG in human skin and cutaneous cells in vitro. We show that DG is present at the epidermal BM zone, and it is produced by both keratinocytes and fibroblasts in vitro. The biosynthetic precursor is…

KeratinocytesCellHuman skinPerlecanDermatologyTransfectionBiochemistryCell LineDystroglycanmedicineExtracellularMyocyteHumansCytoskeletonDystroglycansMolecular BiologyBasement membraneMembrane GlycoproteinsbiologyMembrane ProteinsDermisCell BiologyCell biologyCulture MediaProtein Structure TertiaryCytoskeletal Proteinsmedicine.anatomical_structureBiochemistrybiology.proteinProtein BindingJournal of Investigative Dermatology
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cFLIPL Inhibits Tumor Necrosis Factor-related Apoptosis-inducing Ligand-mediated NF-κB Activation at the Death-inducing Signaling Complex in Human Ke…

2004

Human keratinocytes undergo apoptosis following treatment with tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) via surface-expressed TRAIL receptors 1 and 2. In addition, TRAIL triggers nonapoptotic signaling pathways including activation of the transcription factor NF-kappaB, in particular when TRAIL-induced apoptosis is blocked. The intracellular protein cFLIP(L) interferes with TRAIL-induced apoptosis at the death-inducing signaling complex (DISC) in many cell types. To study the role of cFLIP(L) in TRAIL signaling, we established stable HaCaT keratinocyte cell lines expressing varying levels of cFLIP(L). Functional analysis revealed that relative cFLIP(L) levels correlat…

KeratinocytesCytoplasmReceptor complexCell SurvivalCASP8 and FADD-Like Apoptosis Regulating ProteinApoptosisCell SeparationBiologyCaspase 8Sensitivity and SpecificityBiochemistryProinflammatory cytokineTNF-Related Apoptosis-Inducing LigandRibonucleasesCell Line TumorHumansEnzyme InhibitorsMolecular BiologyTranscription factorSkinInflammationCaspase 8Membrane GlycoproteinsTumor Necrosis Factor-alphaIntracellular Signaling Peptides and ProteinsNF-kappa BCell BiologyFlow CytometryRecombinant ProteinsCell biologyRetroviridaeApoptosisCaspasesDeath-inducing signaling complexRNATumor necrosis factor alphaSignal transductionApoptosis Regulatory ProteinsPropidiumProtein BindingSignal TransductionJournal of Biological Chemistry
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Kininogen binding protein p33/gC1qR is localized in the vesicular fraction of endothelial cells

1996

AbstractThe endothelial protein p33/gC1qR is thought to mediate the assembly of components of the kinin-forming and complement-activating pathways on the surface of cardiovascular cells. FACS analysis of intact human umbilical vein endothelial cells using specific antibodies to p33 revealed a minor fluorescence on the cell surface whereas permeabilized cells showed a bright fluorescence indicative of an intracellular localization of p33. Immunostaining of fixed cells confirmed the predominant intracellular localization of p33. Fractionation studies demonstrated that the vesicular but not the membrane fraction of EA.hy926 cells is rich in p33. We conclude that externalization of p33 must pre…

Kininogen bindingp33Kininogen binding proteinCellBiophysicsComplementFluorescent Antibody TechniqueBiologyBiochemistryUmbilical veinMitochondrial ProteinsStructural BiologyGeneticsmedicineHumansMolecular BiologyCells CulturedMembrane GlycoproteinsImmune SeraCell BiologyKininFlow CytometryKininFluorescenceReceptors ComplementCell biologyEndothelial stem cellSpecific antibodyHyaluronan Receptorsmedicine.anatomical_structuregC1qREndothelium VascularCarrier ProteinsImmunostainingFEBS Letters
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Langerinneg conventional dendritic cells produce IL-23 to drive psoriatic plaque formation in mice.

2013

Psoriasis is an autoinflammatory skin disease of unknown etiology. Topical application of Aldara cream containing the Toll-like receptor (TLR)7 agonist Imiquimod (IMQ) onto patients induces flares of psoriasis. Likewise, in mice IMQ triggers pathological changes closely resembling psoriatic plaque formation. Key cytokines like IL-23 and type-I IFN (IFN-I), both being produced mainly by dendritic cells (DCs), have been implicated in psoriasis. Although plasmacytoid DCs (pDCs) are the main source of IFNα and thought to initiate disease, conventional DCs (cDCs) appear to maintain the psoriatic lesions. Any role of cDCs during lesion formation remains elusive. Here, we report that selective ac…

LangerinCD11c610 Medicine & healthInflammation10263 Institute of Experimental ImmunologyInterleukin-23Mice03 medical and health sciences0302 clinical medicinePsoriasismedicineInterleukin 23AnimalsPsoriasisLectins C-Type030304 developmental biologyMice Knockout1000 Multidisciplinary0303 health sciencesImiquimodMembrane GlycoproteinsMultidisciplinarybiologyintegumentary systemhemic and immune systemsDendritic cellTLR7Biological SciencesAcquired immune systemmedicine.disease3. Good healthDisease Models AnimalMannose-Binding LectinsToll-Like Receptor 7Langerhans Cells030220 oncology & carcinogenesisAntigens SurfaceMyeloid Differentiation Factor 88ImmunologyAminoquinolinesbiology.protein570 Life sciences; biologymedicine.symptom
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Thermodynamics of the Interaction between the Spike Protein of Severe Acute Respiratory Syndrome Coronavirus-2 and the Receptor of Human Angiotensin-…

2020

Since the end of 2019, the coronavirus SARS-CoV-2 has caused more than 1000000 deaths all over the world and still lacks a medical treatment despite the attention of the whole scientific community. Human angiotensin-converting enzyme 2 (ACE2) was recently recognized as the transmembrane protein that serves as the point of entry of SARS-CoV-2 into cells, thus constituting the first biomolecular event leading to COVID-19 disease. Here, by means of a state-of-the-art computational approach, we propose a rational evaluation of the molecular mechanisms behind the formation of the protein complex. Moreover, the free energy of binding between ACE2 and the active receptor binding domain of the SARS…

LetterPneumonia ViralProtein domainThermodynamicsPlasma protein bindingMolecular Dynamics SimulationPeptidyl-Dipeptidase ALigandsmedicine.disease_causeProtein-Protein Binding01 natural sciencesDockingBetacoronavirus03 medical and health sciencesProtein Domains0103 physical sciencesmedicineHumansGeneral Materials SciencePhysical and Theoretical ChemistryBinding siteReceptorPandemics030304 developmental biologyCoronaviruschemistry.chemical_classification0303 health sciencesBinding Sites010304 chemical physicsSARS-CoV-2Spike ProteinCOVID-19PlicamycinTransmembrane proteinEnzymechemistrySettore CHIM/03 - Chimica Generale E InorganicaMolecular Dynamics SimulationsSpike Glycoprotein CoronavirusAngiotensin-converting enzyme 2DiosminThermodynamicsAngiotensin-Converting Enzyme 2Coronavirus InfectionsProtein Binding
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Interaction of TLR2 and TLR4 ligands with the N-terminal domain of Gp96 amplifies innate and adaptive immune responses.

2006

Activation of dendritic cells by ligands for Toll-like receptors (TLR) is a crucial event in the initiation of innate and adaptive immune responses. Several classes of TLR ligands have been identified that interact with distinct members of the TLR-family. TLR4 ligands include lipopolysaccharide derived from different Gram-negative bacteria and viral proteins. Recent reports have demonstrated the TLR-mediated activation of dendritic cells by heat shock proteins (HSPs). However, doubts were raised as to what extent this effect was due to lipopolysaccharide contaminations of the HSP preparations. We re-examined this phenomenon using Gp96 or its N-terminal domain, nominally endotoxin-free (0.5 …

LipopolysaccharidesLipopolysaccharideBiologyCD8-Positive T-LymphocytesBiochemistrychemistry.chemical_compoundMiceImmune systemDogsHeat shock proteinAnimalsHumansReceptorMolecular BiologyInflammationMice Inbred BALB CInnate immune systemMembrane GlycoproteinsCCL18Cell BiologyToll-Like Receptor 2Cell biologyEndotoxinsMice Inbred C57BLToll-Like Receptor 4TLR2BiochemistrychemistryTLR4The Journal of biological chemistry
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