Search results for " Tertiary"

showing 10 items of 349 documents

Light-induced Changes in the Dimerization Interface of Bacteriophytochromes

2015

Phytochromes are dimeric photoreceptor proteins that sense red light levels in plants, fungi, and bacteria. The proteins are structurally divided into a light-sensing photosensory module consisting of PAS, GAF, and PHY domains and a signaling output module, which in bacteriophytochromes typically is a histidine kinase (HK) domain. Existing structural data suggest that two dimerization interfaces exist between the GAF and HK domains, but their functional roles remain unclear. Using mutational, biochemical, and computational analyses of the Deinococcus radiodurans phytochrome, we demonstrate that two dimerization interfaces between sister GAF and HK domains stabilize the dimer with approximat…

Histidine KinaseLightProtein ConformationMutantCrystallography X-RayBiochemistryProtein structureBacterial Proteinsx-ray scatteringcell signalingDeinococcusMolecular BiologybiologyPhytochromeHistidine kinaseMutagenesista1182Photoreceptor proteinDeinococcus radioduransCell Biologybiology.organism_classificationphotoreceptormolecular dynamicsProtein Structure TertiaryBiochemistryhigh performance liquid chromatography (HPLC)BiophysicsDeinococcusPhytochromeDimerizationProtein KinasesmutagenesisMolecular BiophysicsJournal of Biological Chemistry
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Sponge Bcl-2 homologous protein (BHP2-GC) confers distinct stress resistance to human HEK-293 cells

2001

It is established that sponges, the phylogenetically oldest still extant phylum of Metazoa, possess key molecules of the apoptotic pathways, that is members from the Bcl-2 family and a pro-apoptotic molecule with death domains. Here we report on transfection studies of human cells with a sponge gene, GCBHP2. Sponge tissue was exposed to heat shock and tributyltin, which caused an upregulation of gene expression of GCBHP2. The cDNA GCBHP2 was introduced into human HEK-293 cells and mouse NIH-3T3 cells; the stable transfection was confirmed by the identification of the transcripts, by Western blotting as well as by immunofluorescence using antibodies raised against the recombinant polypeptide…

Hot Temperatureanimal structuresCell SurvivalvirusesMolecular Sequence DataDrug ResistanceApoptosisAntibodiesCell LineMiceComplementary DNAGene expressionAnimalsHumansAmino Acid SequenceRNA MessengerCloning MolecularMolecular BiologyPhylogenySequence Homology Amino AcidbiologyCaspase 3ChemistryfungiHEK 293 cellsCell BiologyTransfectionbiology.organism_classificationMolecular biologyPoriferaProtein Structure TertiaryUp-RegulationEnzyme ActivationBlotSpongeProto-Oncogene Proteins c-bcl-2Cell cultureCaspasesembryonic structuresbiology.proteinTrialkyltin CompoundsAntibodySequence AlignmentHeat-Shock ResponseCell Death & Differentiation
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Nouvelles perspectives concernant la structure et la fonction du domaine carboxyl terminal de Hfq

2015

Accumulating evidence indicates that RNA metabolism components assemble into supramolecular cellular structures to mediate functional compartmentalization within the cytoplasmic membrane of the bacterial cell. This cellular compartmentalization could play important roles in the processes of RNA degradation and maturation. These components include Hfq, the RNA chaperone protein, which is involved in the post-transcriptional control of protein synthesis mainly by the virtue of its interactions with several small regulatory ncRNAs (sRNA). The Escherichia coli Hfq is structurally organized into two domains. An N-terminal domain that folds as strongly bent β-sheets within individual protomers to…

IDP intrinsically-disordered proteinslcsh:Lifelcsh:QR1-502sub-membrane macromolecular assemblyPlasma protein bindingsRNA small non-coding RNABiochemistrylcsh:Microbiologyamyloid fibrilsProtein biosynthesis0303 health sciences[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]Escherichia coli Proteins030302 biochemistry & molecular biologyHfqCTRp Hfq C-terminal peptideFTIR Fourier transform infrared spectroscopyNTR N-terminal regionCompartmentalization (psychology)Cell biology[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsRNA Bacterialsmall non-coding ribonucleic acid (RNA)BiochemistryFSD Fourier self-deconvolutionTransfer RNAAmyloid fibrilProtein BindingBiophysicsBiologyHost Factor 1 Protein03 medical and health sciencesEscherichia coliThT thioflavin T[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyProtein Structure QuaternaryncRNA regulatory non-coding RNAPost-transcriptional regulationMolecular Biology030304 developmental biologyOriginal PaperC-terminusRNA[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyCell Biologycellular compartmentalizationWT wild-typeProtein Structure Tertiarylcsh:QH501-531Host Factor 1 ProteinCTR Hfq C-terminal regionribonucleic acid (RNA) processing and degradationBiophysicpost-transcriptional regulationBioscience Reports
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Inhibition of the Cysteine Protease Human Cathepsin L by Triazine Nitriles: Amide⋅⋅⋅Heteroarene π-Stacking Interactions and Chalcogen Bonding in the …

2016

We report an extensive "heteroarene scan" of triazine nitrile ligands of the cysteine protease human cathepsin L (hCatL) to investigate π-stacking on the peptide amide bond Gly67-Gly68 at the entrance of the S3 pocket. This heteroarene⋅⋅⋅peptide bond stacking was supported by a co-crystal structure of an imidazopyridine ligand with hCatL. Inhibitory constants (Ki ) are strongly influenced by the diverse nature of the heterocycles and specific interactions with the local environment of the S3 pocket. Binding affinities vary by three orders of magnitude. All heteroaromatic ligands feature enhanced binding by comparison with hydrocarbon analogues. Predicted energetic contributions from the ori…

ImidazopyridineNitrileStereochemistryCathepsin LPeptideMolecular Dynamics Simulation010402 general chemistryCrystallography X-RayLigands01 natural sciencesBiochemistrychemistry.chemical_compoundAmideDrug DiscoveryHydrolaseNitrilesPeptide bondHumansGeneral Pharmacology Toxicology and PharmaceuticsTriazinePharmacologychemistry.chemical_classificationBinding Sites010405 organic chemistryChemistryLigandTriazinesOrganic ChemistryAmides0104 chemical sciencesProtein Structure TertiaryMolecular MedicineChalcogensQuantum TheoryProtein BindingChemMedChem
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AML-associated Flt3 kinase domain mutations show signal transduction differences compared with Flt3 ITD mutations

2005

Activating mutations of Flt3 are found in approximately one third of patients with acute myeloid leukemia (AML) and are an attractive drug target. Two classes of Flt3 mutations occur: internal tandem duplications (ITDs) in the juxtamembrane and point mutations in the tyrosine kinase domain (TKD). We and others have shown that Flt3-ITD induced aberrant signaling including strong activation of signal transducer and activator of transcription 5 (STAT5) and repression of CCAAT/estradiol-binding protein α (c/EBPα) and Pu.1. Here, we compared the signaling properties of Flt3-ITD versus Flt3-TKD in myeloid progenitor cells. We demonstrate that Flt3-TKD mutations induced autonomous growth of 32D ce…

ImmunologyApoptosisBiologymedicine.disease_causeBiochemistryCell Linefluids and secretionsProto-Oncogene Proteinshemic and lymphatic diseasesSTAT5 Transcription FactormedicineAnimalsHumansPoint MutationMyeloid CellsPhosphorylationProtein kinase BProtein kinase CMutationPoint mutationAutophosphorylationIntracellular Signaling Peptides and ProteinsReceptor Protein-Tyrosine Kinaseshemic and immune systemsCell BiologyHematologyMilk ProteinsStaurosporineMolecular biologyProtein Structure TertiaryDNA-Binding ProteinsMuridaefms-Like Tyrosine Kinase 3Leukemia MyeloidTandem Repeat SequencesAcute Diseaseembryonic structuresFms-Like Tyrosine Kinase 3Mutagenesis Site-DirectedTrans-ActivatorsSignal transductionTyrosine kinaseSignal TransductionTranscription FactorsBlood
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Relationship between within-host fitness and virulence in the vesicular stomatitis virus: correlation with partial decoupling.

2012

ABSTRACT Given the parasitic nature of viruses, it is sometimes assumed that rates of viral replication and dissemination within hosts (within-host fitness) correlate with virulence. However, there is currently little empirical evidence supporting this principle. To test this, we quantified the fitness and virulence of 21 single- or double-nucleotide mutants of the vesicular stomatitis virus in baby hamster kidney cells (BHK-21). We found that, overall, these two traits correlated positively, but significant outliers were identified. Particularly, a single mutation in the conserved C terminus of the N nucleocapsid (U1323A) had a strongly deleterious fitness effect but did not alter or even …

ImmunologyMutantVirulenceApoptosisBiologymedicine.disease_causeVirus ReplicationMicrobiologyVesicular stomatitis Indiana virusCell Line03 medical and health sciencesVesicular StomatitisMiceVirologyCricetinaemedicineBaby hamster kidney cellAnimals030304 developmental biologyGlycoproteinsGenetics0303 health sciencesMutationMice Inbred BALB CVirulence030302 biochemistry & molecular biologyCell MembraneBrainNucleocapsid Proteinsbiology.organism_classification3. Good healthProtein Structure TertiaryViral replicationGenetic Diversity and EvolutionVesicular stomatitis virusInsect ScienceMutationFemaleNeuron deathVesicular StomatitisJournal of virology
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Molecular modeling approaches in the discovery of new drugs for anti-cancer therapy: the investigation of p53-MDM2 interaction and its inhibition by …

2010

The mdm2 oncogene product, MDM2, is an ubiquitin protein ligase that inhibits the transcriptional activity of the tumor suppressor p53 and promotes its degradation. About 50% of all human cancers present mutations or deletions in the TP53 gene. In the remaining half of all human neoplasias that express the wild-type protein, aberrations of p53 regula- tors, such as MDM2, account for p53 inhibition. For this reason, designing small-molecule inhibitors of the p53-MDM2 protein-protein interaction is a promising strategy for the treatment of cancers retaining wild-type p53. The development of inhibitors has been challenging. Although many small-molecule MDM2 inhibitors have shown potent in vitr…

IndolesTumor suppressor geneAntineoplastic AgentsMolecular Dynamics SimulationBioinformaticsBiochemistryGene productNeoplasmsDrug DiscoverymedicineHumansImidazolinesMolecular Modeling New Drugs for Anti-Cancer Therapy p53-MDM2 InteractionPharmacologyBenzodiazepinonesbiologyOncogeneOrganic ChemistryCancerProto-Oncogene Proteins c-mdm2medicine.diseaseSettore CHIM/08 - Chimica FarmaceuticaSmall moleculeUbiquitin ligaseOxindolesProtein Structure TertiaryDrug Designbiology.proteinCancer researchMolecular MedicineMdm2PharmacophoreTumor Suppressor Protein p53Current medicinal chemistry
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Development of novel dipeptide-like rhodesain inhibitors containing the 3-bromoisoxazoline warhead in a constrained conformation.

2015

Novel dipeptide-like rhodesain inhibitors containing the 3-bromoisoxazoline warhead in a constrained conformation were developed; some of them possess K(i) values in the micromolar range. We studied the structure-activity relationship of these derivatives and we performed docking studies, which allowed us to find out the key interactions established by the inhibitors with the target enzyme. Biological results indicate that the nature of the P2 and P3 substituents and their binding to the S2/S3 pockets is strictly interdependent.

InhibitorMolecular modelCell SurvivalClinical BiochemistryTrypanosoma brucei bruceiAntiprotozoal AgentsPharmaceutical ScienceMolecular modelingCysteine Proteinase InhibitorsBiochemistryCell Linechemistry.chemical_compoundMiceStructure-Activity RelationshipCysteine ProteasesDrug DiscoveryAnimalsMolecular Biology3-Bromo isoxazolinechemistry.chemical_classificationDipeptide-likeDipeptideBinding SitesOrganic ChemistryDipeptidesIsoxazolesCombinatorial chemistryProtein Structure TertiaryMolecular Docking SimulationCysteine EndopeptidasesEnzymeRhodesainchemistryWarheadDocking (molecular)Drug DesignMolecular MedicineRhodesain Dipeptide-like 3-Bromo isoxazoline Inhibitor Molecular modelingBioorganicmedicinal chemistry
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A novel putative insect chitinase with multiple catalytic domains: hormonal regulation during metamorphosis

2002

0264-6021 (Print) Journal Article Research Support, Non-U.S. Gov't; We have used differential display to identify genes that are regulated by juvenile hormone in the epidermis of the beetle Tenebrio molitor. One of the genes encodes T. molitor chitinase 5 (TmChit5), a chitinase possessing an unusual structure. Sequence analysis of TmChit5 identified five 'chitinase units' of approx. 480 amino acids with similarity to chitinase family 18. These units are separated by less conserved regions containing putative PEST (rich in proline, glutamic acid, serine and threonine) sequences, putative chitin-binding domains and mucin domains. Northern-blot analysis identified a single transcript of approx…

InsectaMessenger/metabolismBiochemistrychemistry.chemical_compoundCatalytic DomainHormone metabolismNorthernCloning MolecularCycloheximideTenebrioPeptide sequencePhylogenychemistry.chemical_classificationProtein Synthesis InhibitorsDifferential displayBlottingChitinasesMetamorphosis BiologicalAmino acidInsectsBiochemistryProtein Synthesis Inhibitors/pharmacologyInsect ProteinsResearch ArticleProtein StructureDNA ComplementarySequence analysisChitinase/*chemistry/genetics/*metabolismMolecular Sequence DataTenebrio/metabolismMethopreneBiologyComplementary/metabolismAnimalsHormones/*metabolismRNA MessengerAmino Acid SequenceMolecular BiologyGene LibraryInsect Proteins/*chemistry/genetics/*metabolismMetamorphosisGene Expression ProfilingMolecularCell BiologyDNAMethoprene/pharmacologyBlotting NorthernMethopreneBiologicalHormonesProtein Structure TertiarychemistryChitinaseJuvenile hormonebiology.proteinRNACycloheximide/pharmacologyEpidermisTertiaryCloningEpidermis/metabolism
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The Fibril-associated Collagen IX Provides a Novel Mechanism for Cell Adhesion to Cartilaginous Matrix

2004

Collagen IX is the prototype fibril-associated collagen with interruptions in triple helix. In human cartilage it covers collagen fibrils, but its putative cellular receptors have been unknown. The reverse transcription-PCR analysis of human fetal tissues suggested that based on their distribution all four collagen receptor integrins, namely alpha1beta1, alpha2beta1, alpha10beta1, and alpha11beta1, are possible receptors for collagen IX. Furthermore primary chondrocytes and chondrosarcoma cells express the four integrins simultaneously. Chondrosarcoma cells, as well as Chinese hamster ovary cells transfected to express alpha1beta1, alpha2beta1, or alpha10beta1 integrin as their only collage…

Integrin alpha1Integrin alpha2LigandsPolymerase Chain ReactionBiochemistryCollagen receptorMiceCricetinaeReceptorbiologyReverse Transcriptase Polymerase Chain ReactionChemistryChinese hamster ovary cellRecombinant ProteinsCell biologyBiochemistryCollagenIntegrin alpha ChainsProtein BindingMolecular Sequence DataIntegrinChondrosarcomaCHO CellsFibrilCollagen Type IXCell LineChondrocytesMicroscopy Electron TransmissionCell Line TumorCell AdhesionEscherichia coliAnimalsHumansImmunoprecipitationAmino Acid SequenceRNA MessengerBinding siteCell adhesionMolecular BiologyBinding SitesSequence Homology Amino AcidCell BiologyProtein Structure TertiaryRatsMicroscopy ElectronCollagen type I alpha 1CartilageMutationMutagenesis Site-Directedbiology.proteinRNAPeptidesJournal of Biological Chemistry
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