Search results for " secondary"

showing 10 items of 692 documents

Synthesis and Structural Model of an α(2,6)-Sialyl-T Glycosylated MUC1 Eicosapeptide under Physiological Conditions

2006

To study the effect of O-glycosylation on the conformational propensities of a peptide backbone, a 20-residue peptide (GSTAPPAHGVTSAPDTRPAP) representing the full length tandem repeat sequence of the human mucin MUC1 and its analogue glycosylated with the (2,6)-sialyl-T antigen on Thr11, were prepared and investigated by NMR and molecular modeling. The peptides contain both the GVTSAP sequence, which is an effective substrate for GalNAc transferases, and the PDTRP fragment, a known epitope recognized by several anti-MUC1 monoclonal antibodies. It has been shown that glycosylation of threonine in the GVTSAP sequence is a prerequisite for subsequent glycosylation of the serine at GVTSAP. Furt…

Models Molecularchemistry.chemical_classificationMagnetic Resonance SpectroscopyGlycosylationMolecular modelChemistryStereochemistryMucin-1Organic ChemistryGlycopeptidesTemperaturePeptideGeneral ChemistryCatalysisEpitopecarbohydrates (lipids)Turn (biochemistry)chemistry.chemical_compoundSolid-phase synthesisBiochemistryBiomimeticsThermodynamicsIndicators and ReagentsProtein secondary structureMUC1Chemistry - A European Journal
researchProduct

Crystal Structure of Perakine Reductase, Founding Member of a Novel Aldo-Keto Reductase (AKR) Subfamily That Undergoes Unique Conformational Changes …

2012

Perakine reductase (PR) catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. Sequence alignment shows that PR is the founder of the new AKR13D subfamily and is designated AKR13D1. The x-ray structure of methylated His(6)-PR was solved to 2.31 Å. However, the active site of PR was blocked by the connected parts of the neighbor symmetric molecule in the crystal. To break the interactions and obtain the enzyme-ligand complexes, the A213W mutant was generated. The atomic structure of His(6)-PR-A213W complex with NADPH was determined at 1.77 Å. Overal…

Models Molecularendocrine systemConformational changeProtein ConformationStereochemistryReductaseCrystallography X-Raycomplex mixturesMethylationBiochemistryProtein Structure SecondaryRauwolfiaEvolution MolecularProtein structurehemic and lymphatic diseasesheterocyclic compoundsMolecular BiologyAldo-keto reductaseCofactor bindingbiologyChemistryorganic chemicalsActive siteCell BiologyEnzyme structureAlcohol OxidoreductasesCrystallographyProtein Structure and Foldingbiology.proteinNADPH bindingSequence AlignmentNADPProtein BindingJournal of Biological Chemistry
researchProduct

Solution structure of aD,L-alternating oligonorleucine as a model of double-stranded antiparallel ?-helix

2002

Conformational characteristics of alternating D,L linear peptides are of particular interest because of their capacity to form transmembrane channels with different transport properties, as some natural antibiotics do. Single- and double-stranded beta-helical structures are common for alternating D,L peptides. The stability of the beta-helix depends on several structural factors, such as the backbone peptide length, type and position of side chains, and nature of terminal groups. The NMR and molecular dynamics solution conformation of a synthetic alternating D,L-oligopeptide with 15 norleucines (XVMe) has been used as a model to get insight in to the conformational features of double-strand…

Models Molecularenergy minimizationStereochemistryBiophysicsBeta helixStereoisomerismEnergy minimizationAntiparallel (biochemistry)BiochemistryProtein Structure SecondaryBiomaterialsMolecular dynamicsBiopolymerstwo-dimensional NMRProtein structureNorleucineSide chainDL-alternating peptNuclear Magnetic Resonance BiomolecularTransmembrane channelsChemistryOrganic ChemistryStereoisomerismGeneral Medicinemolecular dynamicsCrystallographybeta-helixOligopeptidesBiopolymers
researchProduct

Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase

2017

Sensor histidine kinases are central to sensing in bacteria and in plants. They usually contain sensor, linker, and kinase modules and the structure of many of these components is known. However, it is unclear how the kinase module is structurally regulated. Here, we use nano- to millisecond time-resolved X-ray scattering to visualize the solution structural changes that occur when the light-sensitive model histidine kinase YF1 is activated by blue light. We find that the coiled coil linker and the attached histidine kinase domains undergo a left handed rotation within microseconds. In a much slower second step, the kinase domains rearrange internally. This structural mechanism presents a t…

Models MolecularkinaasitentsyymitHistidine KinaseLightProtein ConformationScienceQCrystallography X-RayArticleProtein Structure SecondaryaktivointiBacterial ProteinsProtein DomainsX-Ray DiffractionphotoactivationScattering Small AngleNanotechnologysensor histidine kinasesNature Communications
researchProduct

Monoclonal antibody to a DNA-binding domain of p53 mimics charge structure of DNA: anti-idiotypes to the anti-p53 antibody are anti-DNA

2004

Antibodies to DNA are important markers of various autoimmune diseases and can be pathogenic; however, their generation is not understood. We previously reported that anti-DNA antibodies could be induced in mice by idiotypic immunization to PAb-421, an antibody to a DNA-binding domain of p53. We now report that two monoclonal antibodies of moderate affinity (K(D) asymptotically equal to 10(-7)), raised from PAb-421-immunized mice, specifically recognized both PAb-421 and DNA. These antibodies feature multiple arginine residues in the antigen-binding site, a unique characteristic of disease-associated anti-DNA antibodies; nevertheless, these anti-DNA antibodies show specific complementarity …

Models Molecularmedicine.drug_classMolecular Sequence DataImmunologyOligonucleotidesMonoclonal antibodyMicechemistry.chemical_compoundImmunoglobulin IdiotypesmedicineAnimalsImmunology and AllergyA-DNAAmino Acid SequencebiologyOligonucleotideAntibodies MonoclonalDNAMolecular biologyPrimary and secondary antibodiesProtein Structure TertiarychemistryMonoclonalbiology.proteinTumor Suppressor Protein p53AntibodyDNAProtein BindingBinding domainEuropean Journal of Immunology
researchProduct

Leucine-58 in the putative 5th helical region of human interleukin (IL)-6 is important for activation of the IL-6 signal transducer, gp130

1995

A model of the tertiary structure of human IL-6, derived from the crystal-structure of granulocyte-colony stimulating factor, reveals a 5th helical region in the loop between the first and second alpha-helix. To investigate the importance of this region for biological activity of IL-6, residues Glu-52, Ser-53, Ser-54, Lys-55, Glu-56, Leu-58, and Glu-60 were individually replaced by alanine. IL-6.Leu-58Ala displayed a 5-fold reduced biological activity on the IL-6 responsive human cell lines XG-1 and A375. This reduction in bioactivity was shown to be due to a decreased capacity of the mutant protein to trigger IL-6 receptor-alpha-chain-dependent binding to the IL-6 signal transducer, gp130.

Models Molecularmedicine.medical_specialtyMolecular Sequence DataBiophysicsBiologyBiochemistryBinding CompetitiveProtein Structure SecondaryMiceStructure-function analysisgp130Structural BiologyMutant proteinAntigens CDLeucineInternal medicineGeneticsmedicineCytokine Receptor gp130Tumor Cells CulturedAnimalsHumansAmino Acid SequenceMolecular BiologyAlanineHybridomasMembrane GlycoproteinsBase SequenceInterleukin-6InterleukinBiological activityCell BiologyReceptors InterleukinGlycoprotein 130Receptors Interleukin-6Protein tertiary structureCell biologyProtein Structure TertiaryEndocrinologyMutationLeucineSignal transductionSequence AlignmentCell DivisionSignal TransductionFEBS Letters
researchProduct

The Minor Capsid Protein VP11 of Thermophilic Bacteriophage P23-77 Facilitates Virus Assembly by Using Lipid-Protein Interactions

2015

ABSTRACT Thermus thermophilus bacteriophage P23-77 is the type member of a new virus family of icosahedral, tailless, inner-membrane-containing double-stranded DNA (dsDNA) viruses infecting thermophilic bacteria and halophilic archaea. The viruses have a unique capsid architecture consisting of two major capsid proteins assembled in various building blocks. We analyzed the function of the minor capsid protein VP11, which is the third known capsid component in bacteriophage P23-77. Our findings show that VP11 is a dynamically elongated dimer with a predominantly α-helical secondary structure and high thermal stability. The high proportion of basic amino acids in the protein enables electrost…

Models MolecularvirusesMolecular Sequence DataStatic ElectricityImmunologyMicrobiologyProtein–protein interactionBacteriophagechemistry.chemical_compoundCapsidVirologyBacteriophagesAmino Acid SequenceThermusPeptide sequenceProtein secondary structureprotein-lipid systemsbiologyVirus AssemblyStructure and AssemblyCapsomereVirionThermus thermophilusLipid Metabolismbiology.organism_classificationLipidsMolecular biologychemistryCapsidInsect Sciencethermophilic virusesBiophysicsCapsid ProteinsDNAkapsidiJournal of Virology
researchProduct

RNA-binding properties and membrane insertion of Melon necrotic spot virus (MNSV) double gene block movement proteins

2006

AbstractAdvances in structural and biochemical properties of carmovirus movement proteins (MPs) have only been obtained in p7 and p9 from Carnation mottle virus (CarMV). Alignment of carmovirus MPs revealed a low conservation of amino acid identity but interestingly, similarity was elevated in regions associated with the functional secondary structure elements reported for CarMV which were conserved in all studied proteins. Nevertheless, some differential features in relation with CarMV MPs were identified in those from Melon necrotic virus (MNSV) (p7A and p7B). p7A was a soluble non-sequence specific RNA-binding protein, but unlike CarMV p7, its central region alone could not account for t…

Molecular Sequence DataSequence alignmentBiologyMembranes (Biologia)VirologyAmino Acid SequencePeptide sequenceProtein secondary structureIntegral membrane proteinPlant DiseasesMelon necrotic spot virusCarmovirusProteïnes de membranaRNA-Binding ProteinsRNAbiology.organism_classificationRNA-binding domainVirusPlant Viral Movement ProteinsCucurbitaceaeMovement proteinsBiochemistryCarnation mottle virusMelon plantsCarmovirusMNSVMembrane insertionSequence AlignmentGene DeletionVirology
researchProduct

Tension causes structural unfolding of intracellular intermediate filaments

2020

AbstractIntermediate filament (IF) proteins are a class of proteins that constitute different filamentous structures in mammalian cells. As such, IF proteins are part of the load-bearing cytoskeleton and support the nuclear envelope. Molecular dynamics simulations have shown that IF proteins undergo secondary structural changes to compensate mechanical loads, which has been confirmed by experimental in vitro studies on IF hydrogels. However, the structural response of intracellular IF to mechanical load has yet to be elucidated in cellulo. Here, we use in situ nonlinear Raman imaging combined with multivariate data analysis to quantify the intracellular secondary structure of the IF cytoske…

Molecular dynamicsMechanical loadbiologyChemistrySelf-healing hydrogelsBiophysicsbiology.proteinVimentinCytoskeletonIntermediate filamentProtein secondary structureIntracellular
researchProduct

On base loci of higher fundamental forms of toric varieties

2019

We study the base locus of the higher fundamental forms of a projective toric variety $X$ at a general point. More precisely we consider the closure $X$ of the image of a map $({\mathbb C}^*)^k\to {\mathbb P}^n$, sending $t$ to the vector of Laurent monomials with exponents $p_0,\dots,p_n\in {\mathbb Z}^k$. We prove that the $m$-th fundamental form of such an $X$ at a general point has non empty base locus if and only if the points $p_i$ lie on a suitable degree-$m$ affine hypersurface. We then restrict to the case in which the points $p_i$ are all the lattice points of a lattice polytope and we give some applications of the above result. In particular we provide a classification for the se…

MonomialAlgebra and Number Theory010102 general mathematicsLattice (group)Toric varietyPolytope01 natural sciencesBase locusBlowing upCombinatoricsMathematics - Algebraic GeometryMathematics::Algebraic GeometryHypersurfaceToric varieties fundamental forms0103 physical sciencesFOS: MathematicsSettore MAT/03 - Geometria010307 mathematical physicsAffine transformation0101 mathematicsAlgebraic Geometry (math.AG)Primary 14M25. Secondary 52B20 53A20MathematicsJournal of Pure and Applied Algebra
researchProduct