Search results for "Protein Domain"

showing 10 items of 132 documents

Binding properties and stability of the Ras-association domain of Rap1-GTP interacting adapter molecule (RIAM).

2012

The Rap1-GTP interacting adapter protein (RIAM) is an important protein in Rap1-mediated integrin activation. By binding to both Rap1 GTPase and talin, RIAM recruits talin to the cell membrane, thus facilitating talin-dependent integrin activation. In this article, we studied the role of the RIAM Ras-association (RA) and pleckstrin-homology (PH) domains in the interaction with Rap1. We found that the RA domain was sufficient for GTP-dependent interaction with Rap1B, and the addition of the PH domain did not change the binding affinity. We also detected GTP-independent interaction of Rap1B with the N-terminus of RIAM. In addition, we found that the PH domain stabilized the RA domain both in …

TalinIntegrinsGTP'lcsh:MedicineGTPaseSignal transductionBiochemistryProtein structureMolecular cell biologyRIAMlcsh:Science0303 health sciencesMultidisciplinarybiologyProtein Stability030302 biochemistry & molecular biologySignal transducing adaptor proteinrap1 GTP-Binding ProteinssitoutuminenCell biologyPleckstrin homology domainRap1Research Articleendocrine systemvuorovaikutusProtein domainIntegrinSignaling in cellular processesPhosphoinositide Signal TransductionSignaling Pathways03 medical and health sciencesCell AdhesionHumansProtein InteractionsBiologyGTPase signaling030304 developmental biologyRas signalingAdaptor Proteins Signal Transducingintegriinitlcsh:RProteinsMembrane ProteinsRegulatory ProteinsProtein Structure TertiaryCytoskeletal Proteinsenzymes and coenzymes (carbohydrates)rap GTP-Binding ProteinsCell movement signalingbiology.proteinta1181lcsh:QPLoS ONE
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A critical evaluation of caplacizumab for the treatment of acquired thrombotic thrombocytopenic purpura

2020

Introduction: Acquired thrombotic thrombocytopenic purpura (aTTP) is a thrombotic microangiopathy caused by inhibitory autoantibodies against ADAMTS13 protein. Until recently, the combination of plasma exchange (PEX) and immunosuppression has been the standard front-line treatment in this disorder. However, aTTP-related mortality, refractoriness, and relapse are still a matter of concern. Areas covered: The better understanding of the pathophysiological mechanisms of aTTP has allowed substantial improvements in the diagnosis and treatment of this disease. Recently, the novel anti-VWF nanobody caplacizumab has been approved for acute episodes of aTTP. Caplacizumab is capable to block the adh…

Thrombotic microangiopathyExacerbationvirusesmedicine.medical_treatmentADAMTS13 ProteinDiseaseBioinformaticsAutoantigens03 medical and health sciencesPlatelet Adhesiveness0302 clinical medicineFibrinolytic AgentsProtein DomainsCrotalid Venomsvon Willebrand FactormedicineHumansImmunologic FactorsMulticenter Studies as TopicLectins C-TypeMolecular Targeted TherapyDrug ApprovalClinical Trials as TopicAcquired Thrombotic Thrombocytopenic PurpuraPlasma ExchangePurpura Thrombotic Thrombocytopenicbusiness.industryStandard treatmentfungiImmunosuppressionDrugs InvestigationalHematologyAptamers NucleotideSingle-Domain Antibodiesbiochemical phenomena metabolism and nutritionmedicine.diseaseCombined Modality TherapyRecombinant ProteinsADAMTS13AcetylcysteineTreatment Outcome030220 oncology & carcinogenesisDrug Therapy CombinationCaplacizumabbusinessImmunosuppressive Agents030215 immunologyExpert Review of Hematology
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Rbt1 Protein Domains Analysis in Candida albicans Brings Insights into Hyphal Surface Modifications and Rbt1 Potential Role during Adhesion and Biofi…

2013

Cell wall proteins are central to the virulence of Candida albicans. Hwp1, Hwp2 and Rbt1 form a family of hypha-associated cell surface proteins. Hwp1 and Hwp2 have been involved in adhesion and other virulence traits but Rbt1 is still poorly characterized. To assess the role of Rbt1 in the interaction of C. albicans with biotic and abiotic surfaces independently of its morphological state, heterologous expression and promoter swap strategies were applied. The N-terminal domain with features typical of the Flo11 superfamily was found to be essential for adhesiveness to polystyrene through an increase in cell surface hydrophobicity. A 42 amino acid-long domain localized in the central part o…

[SDV]Life Sciences [q-bio]lcsh:MedicinebiofilmCell membraneadhésionCandida albicanslcsh:ScienceCandida albicansRecombination Genetic0303 health sciencesFungal proteinMultidisciplinaryCandida albicans;cell wall;protein;Rbt1;adhesion;biofilmbiologyFlow Cytometry3. Good healthCell biologyTransport proteinProtein Transportadhesionmedicine.anatomical_structureprotéineparoi cellulaireHydrophobic and Hydrophilic InteractionsResearch ArticleProtein domainSaccharomyces cerevisiaeHyphaeSaccharomyces cerevisiaeFungal ProteinsStructure-Activity Relationship03 medical and health sciencesCell AdhesionmedicineHumansAmino Acid SequenceCell adhesion030304 developmental biologySequence Homology Amino Acid030306 microbiologyCell Membranelcsh:Rfungibiology.organism_classificationRbt1Protein Structure TertiaryMembrane proteinBiofilmsPolystyrenescell walllcsh:Qprotein
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Toll signal transduction pathway in bivalves: Complete cds of intermediate elements and related gene transcription levels in hemocytes of immune stim…

2014

Based on protein domain structure and organization deduced from mRNA contigs, 15 transcripts of the Toll signaling pathway have been identified in the bivalve, Mytilus galloprovincialis. Identical searches performed on publicly available Mytilus edulis ESTs revealed 11 transcripts, whereas searches performed in genomic and new transcriptome sequences of the Pacific oyster, Crassostrea gigas, identified 21 Toll-related transcripts. The remarkable molecular diversity of TRAF and IKK coding sequences of C. gigas, suggests that the sequence data inferred from Mytilus cDNAs may not be exhaustive. Most of the Toll pathway genes were constitutively and ubiquitously expressed in M. galloprovinciali…

animal structuresMolluskToll signaling pathwayInnate immunity; Mollusks; Mytilus; Signal transduction; Toll pathway; NF-κBImmunologyProtein domainSettore BIO/05 - ZoologiaMytiluSignal transductionNF-κBTranscriptomeTranscription (biology)Animals[SDU.STU.HY]Sciences of the Universe [physics]/Earth Sciences/HydrologyGenePhylogenyComputingMilieux_MISCELLANEOUSMytilusInnate immunityMessenger RNAInnate immune systemMollusksToll-like receptors; signal transduction; Mytilus-galloprovincialis Lmk (bivalvia)biologyEcologyfungiMytilus-galloprovincialis Lmk (bivalvia)biology.organism_classificationMytilusToll-like receptorsCell biologyInnate immunity; Mollusks; Mytilus; NF-κB; Signal transduction; Toll pathwayToll pathwayNF-jBDevelopmental Biology
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Connection between Absorption Properties and Conformational Changes in Deinococcus radiodurans Phytochrome

2014

Phytochromes consist of several protein domains and a linear tetrapyrrole molecule, which interact as a red-light-sensing system. In this study, size-exclusion chromatography and light-scattering techniques are combined with UV-vis spectroscopy to investigate light-induced changes in dimeric Deinococcus radiodurans bacterial phytochrome (DrBphP) and its subdomains. The photosensory unit (DrCBD-PHY) shows an unusually stable Pfr state with minimal dark reversion, whereas the histidine kinase (HK) domain facilitates dark reversion to the resting state. Size-exclusion chromatography reveals that all phytochrome fragments remain as dimers in the illuminated state and dark state. Still, the elut…

biologyPhytochromeProtein ConformationElutionProtein domainHistidine kinaseta1182Deinococcus radioduransSDG 10 - Reduced Inequalitiesbiology.organism_classificationBiochemistryTetrapyrroleProtein Structure Tertiarychemistry.chemical_compoundDark stateBacterial ProteinsBiochemistrychemistry/dk/atira/pure/sustainabledevelopmentgoals/reduced_inequalitiesBiophysicsMoleculeSpectrophotometry UltravioletDeinococcusPhytochromeBiochemistry
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Combinatorial chemistry of  -hairpins

2000

Combinatorial chemistry is expanding rapidly both in terms of chemistry development and application to the synthesis of compound libraries for lead discovery and optimization. Combinatorial technologies continue evolving and developing, in fact they are being used as basic research tools in different fields that include peptide/protein folding. This review examines the use of combinatorial chemistry in the design of peptides and protein domains that adopt beta-sheet conformations. In particular, the use of conformationally restricted peptide libraries has allowed the identification of linear peptides that are folded in a beta-hairpin structure in plain aqueous solutions.

chemistry.chemical_classificationPeptidomimeticChemistryOrganic ChemistryProtein domainPeptideGeneral MedicineCombinatorial chemistryCatalysisPeptide ConformationInorganic ChemistryProtein structureBasic researchDrug DiscoveryProtein foldingPhysical and Theoretical ChemistryPeptide libraryMolecular BiologyInformation SystemsMolecular Diversity
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Design of bioactive and structurally well-defined peptides from conformationally restricted libraries

2004

Libraries of peptides and proteins can be categorized according to the function of their origin in gene- and synthetic-based libraries. Both kinds of libraries have the potential to generate the same grade of molecular diversity, although the limits imposed by the synthetic methods have been lately a matter of discussion. However, the use of synthetic strategies allows incorporation of non-natural amino acids. The development of canfonnallonally restricted synthetic peptide libraries can be considered as a point of convergence of the two methodologies. In these libraries the diversity is grafted into scaffolds that are defined by stable secondary structural motifs, and the deconvolution pro…

chemistry.chemical_classificationPeptidomimeticStereochemistryOrganic ChemistryProtein domainBiophysicsPeptideGeneral MedicineComputational biologyBiochemistryAmino acidBiomaterialsFolding (chemistry)chemistryWell-definedStructural motifFunction (biology)Biopolymers
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Affinity Cleavage of Carbamoyl-Phosphate Synthetase I Localizes Regions of the Enzyme Interacting with the Molecule of ATP that Phosphorylates Carbam…

1995

Two ATP molecules are used in the reaction catalyzed by carbamoyl-phosphate synthetase I. One molecule (ATPA) phosphorylates HCO3- and the other (ATPB) phosphorylates carbamate. Carbamoyl-phosphate synthetase I is a 160-kDa polypeptide consisting of a 40-kDa N-terminal moiety and a 120-kDa C-terminal moiety, the latter being composed of two similar halves of molecular mass 60 kDa. We showed [Alonso, E., Cervera, J., Garcia-Espana, A., Bendala, E. & Rubio, V. (1992) J. Biol. Chem. 267, 4524-4532] that Fe.ATP bound at the site for ATPB catalyzes the oxidative inactivation of carbamoyl-phosphate synthetase I in a model oxidative system consisting of Fe3+, ascorbate, and O2, and we detected ATP…

chemistry.chemical_classificationbiologyChemistryProtein domainCarbamate kinaseCleavage (embryo)BiochemistryCarbamoyl phosphate synthetase IAmino acidBiochemistrybiology.proteinMoietyNucleotideBinding siteEuropean Journal of Biochemistry
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Functional and conformational properties of the exclusive C-domain from the Arabidopsis copper chaperone (CCH)

2001

The Arabidopsis thaliana copper chaperone (CCH) is a small copper binding protein involved in copper trafficking. When compared to homologues from other eukaryotes, CCH has two different domains; the conserved N-domain and the plant-exclusive C-domain, a C-terminal extension with an unusual amino-acid composition. In order to characterize this extra C-domain, the CCH protein, the N-domain and the C-domain were all expressed separately in heterologous systems. While the N-domain retained the copper chaperone and antioxidant properties described for the yeast Atx1 and human HAH1 counterparts, the C-domain displayed particular structural properties that would be necessary to optimize copper ho…

endocrine systemMetallochaperone; Extended structure; Protein domainProtein domain:CIENCIAS DE LA VIDA::Bioquímica [UNESCO]MetallochaperoneUNESCO::CIENCIAS DE LA VIDA::BioquímicaCell BiologyMolecular BiologyBiochemistryExtended structure
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Modeling of the N-terminal Section and the Lumenal Loop of Trimeric Light Harvesting Complex II (LHCII) by Using EPR

2015

The major light harvesting complex II (LHCII) of green plants plays a key role in the absorption of sunlight, the regulation of photosynthesis, and in preventing photodamage by excess light. The latter two functions are thought to involve the lumenal loop and the N-terminal domain. Their structure and mobility in an aqueous environment are only partially known. Electron paramagnetic resonance (EPR) has been used to measure the structure of these hydrophilic protein domains in detergent-solubilized LHCII. A new technique is introduced to prepare LHCII trimers in which only one monomer is spin-labeled. These heterogeneous trimers allow to measure intra-molecular distances within one LHCII mon…

inorganic chemicalsModels MolecularProtein ConformationProtein domainTrimerContext (language use)complex mixturesBiochemistrylaw.inventionchemistry.chemical_compoundBiopolymersProtein structurelawElectron paramagnetic resonanceMolecular BiologySuperhelixfungiElectron Spin Resonance SpectroscopyPhotosystem II Protein ComplexCell Biologyequipment and suppliesCrystallographyMonomerModels ChemicalchemistryThylakoidProtein Structure and FoldingbacteriaJournal of Biological Chemistry
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