Search results for "protein complexes"

showing 10 items of 113 documents

Lhca5 interaction with plant photosystem I

2006

AbstractIn the outer antenna (LHCI) of higher plant photosystem I (PSI) four abundantly expressed light-harvesting protein of photosystem I (Lhca)-type proteins are organized in two heterodimeric domains (Lhca1/Lhca4 and Lhca2/Lhca3). Our cross-linking studies on PSI-LHCI preparations from wildtype Arabidopsis and pea plants indicate an exclusive interaction of the rarely expressed Lhca5 light-harvesting protein with LHCI in the Lhca2/Lhca3-site. In PSI particles with an altered LHCI composition Lhca5 assembles in the Lhca1/Lhca4 site, partly as a homodimer. This flexibility indicates a binding-competitive model for the LHCI assembly in plants regulated by molecular interactions of the Lhca…

Models MolecularPhotosystem IArabidopsisLight-Harvesting Protein ComplexesBiophysicsPhotosystem IBiochemistrychemistry.chemical_compoundLight harvesting complex IStructural BiologyArabidopsisGeneticsMolecular BiologyLhca5Molecular interactionsPhotosystem I Protein ComplexbiologyArabidopsis ProteinsPeasWild typefood and beveragesArabidopsis ProteinsCell BiologyLight-Harvesting Protein Complexesbiology.organism_classificationCrystallographychemistryChlorophyllBiophysicsLight-harvesting complex ICross-linkingFEBS Letters
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The non-bilayer lipid MGDG stabilizes the major light-harvesting complex (LHCII) against unfolding.

2017

Abstract In the photosynthetic apparatus of plants a high proportion of LHCII protein is needed to integrate 50% non-bilayer lipid MGDG into the lamellar thylakoid membrane, but whether and how the stability of the protein is also affected is not known. Here we use single-molecule force spectroscopy to map the stability of LHCII against mechanical unfolding along the polypeptide chain as a function of oligomerization state and lipid composition. Comparing unfolding forces between monomeric and trimeric LHCII demonstrates that the stability does not increase significantly upon trimerization but can mainly be correlated with specific contact sites between adjacent monomers. In contrast, unfol…

Models MolecularProtein ConformationScienceGalactolipidsQRLight-Harvesting Protein ComplexesPeasThylakoidsArticle580 Pflanzen (Botanik)Medicinelipids (amino acids peptides and proteins)580 Botanical sciencesPlant ProteinsProtein UnfoldingScientific reports
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A Quantum Mechanic/Molecular Mechanic Study of the Wild-Type and N155S Mutant HIV-1 Integrase Complexed with Diketo Acid

2008

Integrase (IN) is one of the three human immunodeficiency virus type 1 (HIV-1) enzymes essential for effective viral replication. Recently, mutation studies have been reported that have shown that a certain degree of viral resistance to diketo acids (DKAs) appears when some amino acid residues of the IN active site are mutated. Mutations represent a fascinating experimental challenge, and we invite theoretical simulations for the disclosure of still unexplored features of enzyme reactions. The aim of this work is to understand the molecular mechanisms of HIV-1 IN drug resistance, which will be useful for designing anti-HIV inhibitors with unique resistance profiles. In this study, we use mo…

Models MolecularProtein ConformationStereochemistryBiophysicsIntegrase inhibitorIntegrase InhibitorsHIV IntegraseBiophysical Theory and ModelingMechanicsMolecular mechanicsProtein structureComputer SimulationMagnesiumTernary complexBinding SitesbiologyChemistryAminobutyratesWild typeActive siteLigand (biochemistry)PhenylbutyratesIntegraseModels ChemicalMultiprotein ComplexesMutagenesis Site-Directedbiology.proteinQuantum TheoryProtein BindingBiophysical Journal
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ProteoPlex: stability optimization of macromolecular complexes by sparse-matrix screening of chemical space.

2015

Molecular machines or macromolecular complexes are supramolecular assemblies of biomolecules that ensure cellular homeostasis. Structure determination of those complexes in a purified state is often a tedious undertaking due to the compositional complexity and the related relative structural instability. To improve the stability of macromolecular complexes in vitro, we present here a generic method that optimizes the stability, homogeneity and solubility of macromolecular complexes by sparse-matrix screening of their thermal unfolding behaviour in the presence of various buffers and small molecules. The method includes the automated analysis of thermal unfolding curves based on a newly deve…

Models MolecularProtein FoldingProtein ConformationSupramolecular chemistryBiochemistryArticleProtein structureComputer SimulationMolecular Biologychemistry.chemical_classificationBinding SitesBiomoleculeMolecular biophysicsCell BiologyMolecular machineChemical spacechemistryModels ChemicalChemical physicsMultiprotein ComplexesBiophysicsProtein foldingCrystallizationAlgorithmsSoftwareBiotechnologyMacromoleculeProtein BindingNature methods
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β2 integrin phosphorylation on Thr758 acts as a molecular switch to regulate 14-3-3 and filamin binding

2008

AbstractLeukocyte integrins of the β2 family are essential for immune cell-cell adhesion. In activated cells, β2 integrins are phosphorylated on the cytoplasmic Thr758, leading to 14-3-3 protein recruitment to the β2 integrin. The mutation of this phosphorylation site impairs cell adhesion, actin reorganization, and cell spreading. Thr758 is contained in a Thr triplet of β2 that also mediates binding to filamin. Here, we investigated the binding of filamin, talin, and 14-3-3 proteins to phosphorylated and unphosphorylated β2 integrins by biochemical methods and x-ray crystallography. 14-3-3 proteins bound only to the phosphorylated integrin cytoplasmic peptide, with a high affinity (Kd, 261…

Models MolecularTalinThreonineanimal structuresFilaminsT-LymphocytesStatic ElectricityImmunologyIntegrinCD18macromolecular substancesPlasma protein bindingIn Vitro TechniquesFilaminBiochemistryJurkat Cells03 medical and health sciencesFilamin bindingContractile Proteins0302 clinical medicineCell AdhesionHumansProtein Interaction Domains and MotifsPhosphorylationCell adhesion030304 developmental biology0303 health sciencesBinding SitesbiologyChemistryMicrofilament ProteinsCell BiologyHematologyIntercellular Adhesion Molecule-1Talin bindingRecombinant ProteinsCell biology14-3-3 ProteinsAmino Acid SubstitutionCD18 AntigensMultiprotein Complexes030220 oncology & carcinogenesisbiology.proteinPhosphorylationProtein BindingBlood
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Site-specific incorporation of perylene into an N-terminally modified light-harvesting complex II.

2010

Employing the utility of the native chemical ligation, site-specific attachment of an ultrastable perylene dye to a derivative of the major light-harvesting complex (LHCII) was demonstrated. Biochemical analysis of the conjugate indicated that the structure and function of LHCII remain largely unaffected by the N-terminal modification.

Molecular Sequence DataLight-Harvesting Protein Complexes010402 general chemistryPhotochemistry01 natural sciencesBiochemistry03 medical and health scienceschemistry.chemical_compoundPhysical and Theoretical ChemistryFLUORESCENCEPROTEIN LIGATIONPerylene030304 developmental biologyFluorescent DyesPlant Proteins0303 health sciencesSTABILITYOrganic ChemistryMICROSCOPYPlantsNative chemical ligationFluorescenceLIVE CELLS0104 chemical sciencesStructure and functionchemistryBiophysicsSMALL-MOLECULE PROBESCYSTEINEPeryleneDerivative (chemistry)DYESCysteineConjugateLight harvesting complex IIOrganicbiomolecular chemistry
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Deregulation of the EGFR/PI3K/PTEN/Akt/mTORC1 pathway in breast cancer: possibilities for therapeutic intervention

2014

// Nicole M. Davis 1 , Melissa Sokolosky 1 , Kristin Stadelman 1 , Stephen L. Abrams 1 , Massimo Libra 2 , Saverio Candido 2 , Ferdinando Nicoletti 2 , Jerry Polesel 3 , Roberta Maestro 4 , Antonino D’Assoro 5 , Lyudmyla Drobot 6 , Dariusz Rakus 7 , Agnieszka Gizak 7 , Piotr Laidler 8 , Joanna Dulinska-Litewka 8 , Joerg Basecke 9 , Sanja Mijatovic 10 , Danijela Maksimovic-Ivanic 10 , Giuseppe Montalto 11,12 , Melchiorre Cervello 12 , Timothy L. Fitzgerald 13 , Zoya N. Demidenko 14 , Alberto M. Martelli 15 , Lucio Cocco 15 , Linda S. Steelman 1 and James A. McCubrey 1 1 Department of Microbiology and Immunology, Brody School of Medicine at East Carolina University Greenville, NC 27858 USA 2 …

Oncologymedicine.medical_specialtytherapy resistanceClass I Phosphatidylinositol 3-Kinasesmedicine.medical_treatmentBreast NeoplasmsReviewBiologyMechanistic Target of Rapamycin Complex 1PI3KMetastasisTargeted therapyPhosphatidylinositol 3-KinasesBreast cancerTARGETED THERAPYInternal medicinemedicinePTENHumansTargeted Therapy Therapy Resistance Mutations PI3K mTOR rapamycinskin and connective tissue diseasesProtein kinase BneoplasmsPI3K/AKT/mTOR pathwayRoswell Park Cancer InstituterapamycinTOR Serine-Threonine KinasesMTORPTEN PhosphohydrolaseCancerTargeted TherapyTherapy Resistancemedicine.diseaseTargeted Therapy; Therapy Resistance; Mutations; PI3K; mTOR; rapamycin3. Good healthErbB ReceptorsGene Expression Regulation NeoplasticOncologyMultiprotein ComplexesCancer researchbiology.proteinFemaleReceptor Epidermal Growth FactormutationRAPAMYCINProto-Oncogene Proteins c-aktMutationsSignal Transduction
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"DEVELOPMENT OF A DECISION SUPPORT SYSTEM FOR BIOINFORMATICS. EXTRACTION OF PROTEIN COMPLEXES FROM A PROTEIN-PROTEIN INTERACTION NETWORK: A CASE STUD…

2011

Decision Support Systems and Workflow Management Systems have become essential tools for some business and scientific field. This thesis propose a new hybrid architecture for problem solving expertise and decision-making process, that aims to support high-quality research in the field of bioinformatics and system biology. The first part of the dissertation introduces the project to which belong this thesis work, i.e. the “Bioinformatics Organized Resources - an Intelligent System” (BORIS) project of the ICAR-CNR; the main goal of BORIS is to provide an helpful and effective support to researchers or experimentalist, that have no familiarity with tools and techniques to solve computational p…

PROTEIN COMPLEXESSettore ING-INF/05 - Sistemi Di Elaborazione Delle InformazioniBIOINFORMATICS
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Htid-1, the human homolog of the Drosophila melanogaster l(2)tid tumor suppressor, defines a novel physiological role of APC.

2007

Htid-1, the human counterpart of the Drosophila tumor suppressor gene lethal(2)tumorous imaginal discs (l(2)tid) encodes three splice forms translated into three cytosolic - Tid50, Tid48 and Tid46 - and three mitochondrial - Tid43, Tid40 and Tid38 - proteins. Here we provide evidence for the association of the endogenous Tid50/Tid48 proteins with the adenomatous polyposis coli (APC) tumor suppressor in normal colon epithelium, colorectal cancer cells and mouse NIH3T3 fibroblasts. Using the Glutathione S-transferase binding assay we show that the N-terminal region including the Armadillo domain (ARM) of APC is sufficient to bind the Tid molecules. Using immunoprecipitation and confocal micro…

Patched ReceptorsBeta-cateninTumor suppressor geneAdenomatous polyposis coliAdenomatous Polyposis Coli ProteinReceptors Cell SurfacePlasma protein bindingLigandsMitochondrial ProteinsMiceCytosolCell Line TumorAnimalsDrosophila ProteinsGuanine Nucleotide Exchange FactorsHumansIntestinal MucosaActinHeat-Shock Proteinsbeta CateninPatched ReceptorsbiologySequence Homology Amino AcidGene Expression ProfilingTumor Suppressor ProteinsWnt signaling pathwayGene Expression Regulation DevelopmentalCell BiologyHSP40 Heat-Shock ProteinsActin cytoskeletonMolecular biologyCell biologyMitochondriaDrosophila melanogasterras GTPase-Activating ProteinsMultiprotein Complexesbiology.proteinNIH 3T3 CellsRho Guanine Nucleotide Exchange FactorsProtein BindingCellular signalling
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Recombinant water-soluble chlorophyll protein from Brassica oleracea var. Botrys binds various chlorophyll derivatives.

2003

A gene coding for water-soluble chlorophyll-binding protein (WSCP) from Brassica oleracea var. Botrys has been used to express the protein, extended by a hexahistidyl tag, in Escherichia coli. The protein has been refolded in vitro to study its pigment binding behavior. Recombinant WSCP was found to bind two chlorophylls (Chls) per tetrameric protein complex but no carotenoids in accordance with previous observations with the native protein [Satoh, H., Nakayama, K., Okada, M. (1998) J. Biol. Chem. 273, 30568-30575]. WSCP binds Chl a, Chl b, bacteriochlorophyll a, and the Zn derivative of Chl a but not pheophytin a, indicating that the central metal ion in Chl is essential for binding. WSCP …

PheophytinChlorophyllProtein FoldingDNA PlantLightTetrameric proteinPhotochemistryPigment bindingPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesProtoporphyrinsmacromolecular substancesBrassicaBiologyBiochemistrychemistry.chemical_compoundPigmentPhytolpolycyclic compoundsChlorophyll bindingChlorophyllidesSinglet OxygenCircular DichroismElectron Spin Resonance Spectroscopyfood and beveragesWaterCarotenoidsRecombinant ProteinsBiochemistrychemistrySolubilitySpectrophotometryChlorophyllvisual_artvisual_art.visual_art_mediumProtein foldingSpin LabelsOxidation-ReductionBiochemistry
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