Search results for " Tertiary"

showing 10 items of 349 documents

The collagen receptor subfamily of the integrins

2003

The four collagen receptor integrins, alpha1beta1, alpha2beta1, alpha10beta1 and alpha11beta1, form a structurally and functionally distinct subgroup when compared to other members of the integrin family. In this review, we discuss the structures of these receptors and their differences in collagen binding and signalling function.

IntegrinsReceptors CollagenSubfamilybiologyChemistryIntegrinCell BiologyPlasma protein bindingLigandsBiochemistryProtein Structure TertiaryCollagen receptorCell biologyIntegrin alpha Mbiology.proteinAnimalsHumansSignal transductionReceptorFunction (biology)Protein BindingSignal TransductionThe International Journal of Biochemistry & Cell Biology
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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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The cell adhesion domain of type XVII collagen promotes integrin-mediated cell spreading by a novel mechanism.

2001

Type XVII collagen (BP180) is a keratinocyte transmembrane protein that exists as the full-length protein in hemidesmosomes and as a 120-kDa shed ectodomain in the extracellular matrix. The largest collagenous domain of type XVII collagen, COL15, has been described previously as a cell adhesion domain (Tasanen, K., Eble, J. A., Aumailley, M., Schumann, H., Baetge, J, Tu, H., Bruckner, P., and Bruckner-Tuderman, L. (2000) J. Biol. Chem. 275, 3093-3099). In the present work, the integrin binding of triple helical, human recombinant COL15 was tested. Solid phase binding assays using recombinant integrin alpha(1)I, alpha(2)I, and alpha(10)I domains and cell spreading assays with alpha(1)beta(1)…

KeratinocytesIntegrinsDNA ComplementaryDystoninIntegrinAmino Acid MotifsNerve Tissue ProteinsCHO CellsBiochemistryAutoantigensCollagen receptorCell LineCell MovementCricetinaeCell AdhesionTumor Cells CulturedAnimalsHumansCloning MolecularCell adhesionMolecular BiologyIntegrin bindingbiologyDose-Response Relationship DrugReverse Transcriptase Polymerase Chain ReactionHemidesmosomeCell BiologyNon-Fibrillar CollagensMolecular biologyRecombinant ProteinsProtein Structure TertiaryFibronectinHaCaTCytoskeletal ProteinsEctodomainbiology.proteinCollagenCarrier ProteinsPeptidesProtein BindingThe Journal of biological chemistry
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Induction of Cell Differentiation in Transformed Keratinocytes by Synthetic (Glyco)peptides from the Homophilic Recognition Domain of E-Cadherin

2002

KeratinocytesProtein ConformationCadherinChemistryStereochemistryCellular differentiationMolecular Sequence DataGlycopeptidesCell DifferentiationGeneral ChemistryCadherinsPeptide FragmentsCatalysisGlycopeptideProtein Structure TertiaryDomain (software engineering)Cell biologySolid-phase synthesisMicroscopy FluorescenceHumansAmino Acid SequenceNuclear Magnetic Resonance BiomolecularCell Line TransformedAngewandte Chemie International Edition
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Thermal aggregation of bovine serum albumin at different pH: comparison with human serum albumin.

2007

We report here a study on thermal aggregation of BSA at two different pH values selected to be close to the isoelectric point (pI) of this protein. Our aim is to better understand the several steps and mechanisms accompanying the aggregation process. For this purpose we have performed kinetics of integrated intensity emission of intrinsic and extrinsic dyes, tryptophans and ANS respectively, kinetics of Rayleigh scattering and of turbidity. The results confirm the important role played by conformational changes in the tertiary structure, especially in the exposure of internal hydrophobic regions that promote intermolecular interactions. We also confirm that the absence of electrostatic repu…

KineticsBiophysicsSerum albuminPlasma protein bindingProtein structuremedicineAnimalsHumansScattering RadiationIsoelectric PointBovine serum albuminSerum AlbuminbiologyChemistryCircular DichroismTryptophanSerum Albumin BovineGeneral MedicineHuman serum albuminProtein tertiary structureProtein Structure TertiaryIsoelectric pointBiochemistrybiology.proteinBiophysicsCattlemedicine.drugProtein Binding
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The stem rust resistance gene Rpg5 encodes a protein with nucleotide-binding-site, leucine-rich, and protein kinase domains

2008

We isolated the barley stem rust resistance genes Rpg5 and rpg4 by map-based cloning. These genes are colocalized on a 70-kb genomic region that was delimited by recombination. The Rpg5 gene consists of an unusual structure encoding three typical plant disease resistance protein domains: nucleotide-binding site, leucine-rich repeat, and serine threonine protein kinase. The predicted RPG5 protein has two putative transmembrane sites possibly involved in membrane binding. The gene is expressed at low but detectable levels. Posttranscriptional gene silencing using VIGS resulted in a compatible reaction with a normally incompatible stem rust pathogen. Allele sequencing also validated the candi…

LRP1BSerine threonine protein kinaseBiologyGenes PlantSYT1LeucineHSPA2SNAP23Gene SilencingCloning MolecularPlant DiseasesPlant ProteinsTAF15HSPA9GeneticsBinding SitesMultidisciplinaryPlant StemsNucleotidesFungifood and beveragesHordeumBiological SciencesPhysical Chromosome MappingProtein Structure TertiaryGPS2Protein KinasesProceedings of the National Academy of Sciences
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Is the Rigidity of SARS-CoV-2 Spike Receptor-Binding Motif the Hallmark for Its Enhanced Infectivity? Insights from All-Atom Simulations

2020

The severe acute respiratory syndrome coronavirus (SARS-CoV-2) pandemic is setting the global health crisis of our time, causing a devastating societal and economic burden. An idiosyncratic trait of coronaviruses is the presence of spike glycoproteins on the viral envelope, which mediate the virus binding to specific host receptor, enabling its entry into the human cells. In spite of the high sequence identity of SARS-CoV-2 with its closely related SARS-CoV emerged in 2002, the atomic-level determinants underlining the molecular recognition of SARS-CoV-2 to the angiotensin-converting enzyme 2 (ACE2) receptor and, thus, the rapid virus spread into human body, remain unresolved. Here, multi-m…

LettervirusesAmino Acid MotifsPneumonia ViralVirus Attachment02 engineering and technologyPlasma protein bindingBiologyPeptidyl-Dipeptidase AMolecular Dynamics SimulationVirus03 medical and health sciencesBetacoronavirusViral ProteinsProtein structureViral envelopeGlobal healthHumansGeneral Materials SciencePhysical and Theoretical ChemistryReceptorProtein Structure QuaternaryPandemics030304 developmental biologyGlycoproteinschemistry.chemical_classificationGeneticsInfectivity0303 health sciencesSARS-CoV-2virus diseasesCOVID-19Hydrogen Bonding021001 nanoscience & nanotechnologySARS VirusProtein Structure TertiarySevere acute respiratory syndrome-related coronaviruschemistrySettore CHIM/03 - Chimica Generale E InorganicaQuantum TheoryAngiotensin-Converting Enzyme 20210 nano-technologyGlycoproteinCoronavirus InfectionsProtein Binding
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Characterization of the nucleation process of lysozyme at physiological pH: Primary but not sole process

2013

We report on a kinetic study of the heat-induced aggregation process of lysozyme at physiological pH. The time evolution of the aggregation extent and the conformational changes of the protein were followed by dynamic light scattering (DLS) and FTIR spectroscopy, respectively, whereas the morphology of the aggregates was observed by Atomic Force Microscopy (AFM). The conformational changes of the secondary and tertiary structures were simultaneous and distinct in time with respect to the formation of aggregates. Oligomer formation occurred through at least two different aggregation processes: a nucleation process and a homogeneous non-nucleative diffusion-controlled process. FTIR measuremen…

LightNucleation proceBiophysicsSupramolecular chemistryNucleationmacromolecular substancesProtein aggregationMicroscopy Atomic ForceBiochemistryOligomerProtein Structure Secondarychemistry.chemical_compoundDynamic light scatteringSpectroscopy Fourier Transform InfraredAnimalsScattering RadiationFourier transform infrared spectroscopyCircular DichroismOrganic ChemistryTemperaturetechnology industry and agricultureHydrogen-Ion ConcentrationProtein Structure TertiaryAmorphous solidFTIR spectroscopyCrystallographychemistryChemical engineeringDynamic light scatteringMuramidaseAFMProtein aggregationLysozymeChickensBiophysical Chemistry
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Light-Induced Protein-Matrix Uncoupling and Protein Relaxation in Dry Samples of Trehalose-Coated MbCO at Room Temperature

2005

In humid samples of trehalose-coated carboxy-myoglobin (MbCO), thermally driven conformational relaxation takes place after photodissociation of the carbon monoxide (CO) molecule at room temperature. In such samples, because of the extreme viscosity of the external matrix, photodissociated CO cannot diffuse out of the protein and explores the whole (proximal and distal side) heme pocket, experiencing averaged protein heme pocket structures, as a result of the presence of Brownian motions. At variance, in very dry samples, a lower portion of the photodissociated CO diffuses from the distal to the proximal heme pocket side probing in nonaveraged structures. We revisit here the flash photolysi…

LightProtein ConformationBiophysicsBiochemistrychemistry.chemical_compoundProtein structureAnimalsHumansHemePhotolysisMyoglobinHydrogen bondLasersPhotodissociationRelaxation (NMR)TrehaloseHydrogen BondingCell BiologyGeneral MedicineProtein Structure TertiaryCrystallographychemistryMyoglobinFlash photolysisProtein BindingCarbon monoxideCell Biochemistry and Biophysics
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Quantification of the Raf-C1 Interaction With Solid-Supported Bilayers

2002

By use of the quartz crystal microbalance technique, the interaction of the Raf-Ras binding domain (RafRBD) and the cysteine-rich domain Raf-C1 with lipids was quantified by using solid-supported bilayers immobilized on gold electrodes deposited on 5 MHz quartz plates. Solid-supported lipid bilayers were composed of an initial octanethiol monolayer chemisorbed on gold and a physisorbed phospholipid monolayer varying in its lipid composition as the outermost layer. The integrity of bilayer preparation was monitored by impedance spectroscopy. For binding experiments, a protein construct comprising the RafRBD and Raf-C1 linked to the maltose binding protein and a His tag, termed MBP-Raf-C1, wa…

Lipid BilayersPhospholipidBiosensing TechniquesMicroscopy Atomic ForceBiochemistrychemistry.chemical_compoundMonolayerLipid bilayerMolecular BiologyBilayerOrganic ChemistryUnithiolQuartz crystal microbalanceProtein Structure TertiaryProto-Oncogene Proteins c-rafDissociation constantCrystallographychemistryThermodynamicsMolecular Medicinelipids (amino acids peptides and proteins)AdsorptionGoldDimyristoylphosphatidylcholineProtein adsorptionBinding domainChemBioChem
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