Search results for "Protein structure"

showing 10 items of 757 documents

Procollagen C-proteinase Enhancer Stimulates Procollagen Processing by Binding to the C-propeptide Region Only*

2011

Background: Procollagen C-proteinase enhancer-1 (PCPE-1) is an extracellular glycoprotein that increases activity of certain zinc metalloproteinases involved in tissue development and repair. Results: PCPE-1 binds uniquely to the C-propeptide region of the procollagen molecule. Conclusion: PCPE-1 enhances proteolysis by binding solely to the procollagen C-propeptides. Significance: These data may lead to future applications in the development of antifibrotic therapies.

animal structuresGlycosylationBiologyBiochemistryBone morphogenetic protein 1Protein Structure SecondaryBone Morphogenetic Protein 103 medical and health scienceschemistry.chemical_compoundMetalloprotease0302 clinical medicineHumansBinding siteEnhancerMolecular Biology030304 developmental biologyCell Line TransformedGlycoproteinschemistry.chemical_classification0303 health sciencesMetalloproteinaseExtracellular Matrix ProteinsBinding Sitesintegumentary systemCell BiologyEnzymatic ProcessingFibrosisExtracellular MatrixProcollagen peptidaseCollagen Type IIIchemistryBiochemistry030220 oncology & carcinogenesisembryonic structuresEnzymologyCollagenGlycoproteinProtein Processing Post-TranslationalTriple helixThe Journal of Biological Chemistry
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A synthetic derivative of antimicrobial peptide holothuroidin 2 from mediterranean sea cucumber (Holothuria tubulosa) in the control of Listeria mono…

2019

Due to the limited number of available antibiotics, antimicrobial peptides (AMPs) are considered antimicrobial candidates to fight difficult-to-treat infections such as those associated with biofilms. Marine environments are precious sources of AMPs, as shown by the recent discovery of antibiofilm properties of Holothuroidin 2 (H2), an AMP produced by the Mediterranean sea cucumber Holothuria tubulosa. In this study, we considered the properties of a new H2 derivative, named H2d, and we tested it against seven strains of the dangerous foodborne pathogen Listeria monocytogenes. This peptide was more active than H2 in inhibiting the growth of planktonic L. monocytogenes and was able to interf…

antimicrobial peptideAntibioticsSettore BIO/05 - ZoologiaPharmaceutical SciencePeptideSettore BIO/19 - Microbiologia Generalemedicine.disease_cause01 natural sciencesFoodborne DiseasesDrug DiscoveryListeriosislcsh:QH301-705.5Pharmacology Toxicology and Pharmaceutics (miscellaneous)chemistry.chemical_classification0303 health sciencesbiologyBiofilmFoodborne pathogenAntimicrobialHolothuria tubulosaAnti-Bacterial AgentsSettore CHIM/03 - Chimica Generale E InorganicaAntimicrobial peptidesmedicine.drug_classAntimicrobial peptides-Microbial Sensitivity TestsMolecular Dynamics SimulationArticleMicrobiology03 medical and health sciencesListeria monocytogenesDrug Resistance BacterialmedicineMediterranean SeaAnimalsHolothuria<i>Holothuria tubulosa</i>Listeria monocytogene030304 developmental biology010405 organic chemistryHolothuria tubulosaBiofilmbiology.organism_classificationSettore CHIM/08 - Chimica FarmaceuticaListeria monocytogenesProtein tertiary structure0104 chemical sciencesProtein Structure TertiaryFoodborne pathogenslcsh:Biology (General)chemistryBiofilmsDrug Design<i>Listeria monocytogenes</i>Antimicrobial Cationic Peptides
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High resolution crystal structures of triosephosphate isomerase complexed with its suicide inhibitors: The conformational flexibility of the catalyti…

2011

The key residue of the active site of triosephosphate isomerase (TIM) is the catalytic glutamate, which is proposed to be important (i) as a catalytic base, for initiating the reaction, as well as (ii) for the subsequent proton shuttling steps. The structural properties of this glutamate in the liganded complex have been investigated by studying the high resolution crystal structures of typanosomal TIM, complexed with three suicide inhibitors: (S)-glycidol phosphate ((S)-GOP, at 0.99 A resolution), (R)-glycidol phosphate, ((R)-GOP, at 1.08 A resolution), and bromohydroxyacetone phosphate (BHAP, at 1.97 A resolution). The structures show that in the (S)-GOP active site this catalytic glutama…

biologyChemistryStereochemistryActive siteGlutamic acidIsomeraseBiochemistryTriosephosphate isomerasechemistry.chemical_compoundProtein structureCatalytic cycleSide chainbiology.proteinCarboxylateMolecular BiologyProtein Science
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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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Conformational dynamics of full-length inducible human Hsp70 derived from microsecond molecular dynamics simulations in explicit solvent

2013

Human 70 kDa heat shock protein (hHsp70) is an ATP-dependent chaperone and is currently an important target for developing new drugs in cancer therapy. Knowledge of the conformations of hHsp70 is central to understand the interactions between its nucleotide-binding domain (NBD) and substrate-binding domain (SBD) and is a prerequisite to design inhibitors. The conformations of ADP-bound (or nucleotide-free) hHsp70 and ATP-bound hHsp70 was investigated by using unbiased all-atom molecular dynamics (MD) simulations of homology models of hHsp70 in explicit solvent on a timescale of .5 and 2.7 μs, respectively. The conformational heterogeneity of hHsp70 was analyzed by computing effective free-e…

biologyProtein ConformationChemistrySmall-angle X-ray scatteringScatteringGeneral MedicineMolecular Dynamics SimulationSolventMicrosecondMolecular dynamicsProtein structureFörster resonance energy transferStructural BiologyComputational chemistryChemical physicsChaperone (protein)Scattering Small AngleSolventsbiology.proteinHumansHSP70 Heat-Shock ProteinsProtein Interaction Domains and MotifsMolecular Biology
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The NreA Protein Functions as a Nitrate Receptor in the Staphylococcal Nitrate Regulation System

2013

Staphylococci are able to use nitrate as an alternative electron acceptor during anaerobic respiration. The regulation of energy metabolism is dependent on the presence of oxygen and nitrate. Under anaerobic conditions, staphylococci employ the nitrate regulatory element (Nre) for transcriptional activation of genes involved in reduction and transport of nitrate and nitrite. Of the three proteins that constitute the Nre system, NreB has been characterized as an oxygen sensor kinase and NreC has been characterized as its cognate response regulator. Here, we present structural and functional data that establish NreA as a new type of nitrate receptor. The structure of NreA with bound nitrate w…

chemistry.chemical_classificationAnaerobic respirationStaphylococcusIodideIsothermal titration calorimetryGene Expression Regulation BacterialElectron acceptorCrystallography X-RayResponse ElementsNitrate reductaseNitrate ReductaseProtein Structure SecondaryBacteria Anaerobicchemistry.chemical_compoundResponse regulatorNitratechemistryBiochemistryStructural BiologyMutationBinding siteMolecular BiologyJournal of Molecular Biology
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Structural Properties of Carnation Mottle Virus p7 Movement Protein and Its RNA-binding Domain

2001

Plant viral movement proteins (MPs) participate actively in the intra- and intercellular movement of RNA plant viruses to such an extent that MP dysfunction impairs viral infection. However, the molecular mechanism(s) of their interaction with cognate nucleic acids are not well understood, partly due to the lack of structural information. In this work, a protein dissection approach was used to gain information on the structural and RNA-binding properties of this class of proteins, as exemplified by the 61-amino acid residue p7 MP from carnation mottle virus (CarMV). Circular dichroism spectroscopy showed that CarMV p7 is an alpha/beta RNA-binding soluble protein. Using synthetic peptides de…

chemistry.chemical_classificationBinding SitesCarlavirusC-terminusMolecular Sequence DataRNA-Binding ProteinsRNACell BiologyBiologyAlanine scanningBiochemistryProtein Structure SecondaryAmino acidViral ProteinsProtein structureBiochemistrychemistryRNAAmino Acid SequenceBinding siteMolecular BiologyPeptide sequenceBinding domainJournal of Biological Chemistry
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Proteolytic cleavage of soybean Bowman-Birk inhibitor monitored by means of high-performance capillary electrophoresis. Implications for the mechanis…

1996

The hydrolysis of the soybean Bowman-Birk inhibitor in the presence of catalytic amounts of bovine trypsin and the formation of the non-covalent enzyme-inhibitor complex with an equimolar amount of enzyme are monitored by means of high-performance capillary electrophoresis (HPCE). The inhibitor is cleaved in the trypsin-reactive and more slowly in the chymotrypsin-reactive subdomain. HPCE proves itself as the only reliable analytical tool to monitor these reactions in clear contrast to classical electrophoretic, chromatographic and enzymatic methods. The most efficient separation of the intact and the two active site cleaved forms of the inhibitor was achieved in borate buffer at pH 10.0. T…

chemistry.chemical_classificationBinding SitesChromatographybiologyChemistryHydrolysisMolecular Sequence DataBiophysicsElectrophoresis CapillaryActive siteCleavage (embryo)BiochemistryCatalysisProtein Structure TertiaryKineticsElectrophoresisHydrolysisReaction rate constantEnzymeCapillary electrophoresisBiochemistryEnzyme inhibitorbiology.proteinAmino Acid SequenceTrypsin Inhibitor Bowman-Birk SoybeanJournal of Biochemical and Biophysical Methods
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Hierarchical structure formation of cylindrical brush polymer-surfactant complexes.

2009

The complex formation of cylindrical brush polymers with poly(l-lysine) side chains (PLL) and sodium dodecyl sulfate (SDS) can induce a helical conformation of the cylindrical brush polymer in aqueous solution (Gunari, N.; Cong, Y.; Zhang, B.; Fischer, K.; Janshoff, A.; Schmidt, M. Macromol. Rapid Commun. 2008, 29, 821-825). Herein, we have systematically investigated the influence of surfactant, salt, and pH on the supramolecular structure formation. The cylindrical brush polymers and their complexes with surfactants were directly visualized by atomic force microscopy in air and in aqueous solution. The alkyl chain length (measured by the carbon number, n) of the surfactant plays a key rol…

chemistry.chemical_classificationCircular dichroismAqueous solutionMolecular StructureChemistryPolymersSupramolecular chemistrySurfaces and InterfacesPolymerHydrogen-Ion ConcentrationCondensed Matter PhysicsMicroscopy Atomic ForceProtein Structure Secondarychemistry.chemical_compoundSurface-Active AgentsPulmonary surfactantPolymer chemistryElectrochemistrySide chainGeneral Materials ScienceSodium dodecyl sulfateSpectroscopyAlkylLangmuir : the ACS journal of surfaces and colloids
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Conformational investigation of α,β-dehydropeptides VII*. Conformation of Ac-Pro-ΔAla-NHCH3 and Ac-Pro-(E)-ΔAbu-NHCH3: comparison with (Z)-substitute…

2009

The crystal structure and solution conformation of Ac-Pro-deltaAla-NHCH3 and the solution conformation of Ac-Pro-(E)-deltaAbu-NHCH3 were investigated by X-ray diffraction method and NMR, FTIR and CD spectroscopies. Ac-Pro-deltaAla-NHCH3 adopts an extended-coil conformation in the crystalline state, with all-trans peptide bonds and the deltaAla residue being in a C5 form, phi(1)=-71.4(4), psi(1)=-16.8(4), phi(2)= -178.4(3) and psi(2)= 172.4(3) degrees. In inert solvents the peptide also assumes the C5 conformation, but a gamma-turn on the Pro residue cannot be ruled out. In these solvents Ac-Pro-(E)-deltaAbu-NHCH3 accommodates a beta(II)-turn, but a minor conformer with a nearly planar dispo…

chemistry.chemical_classificationCircular dichroismChemistryStereochemistryStereoisomerismPeptideNuclear magnetic resonance spectroscopyBiochemistrychemistry.chemical_compoundCrystallographyProtein structureDehydroalaninePeptide bondConformational isomerismInternational Journal of Peptide and Protein Research
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