Search results for "Matrix"

showing 10 items of 3205 documents

Structure of an outer surface lipoprotein BBA64 from the Lyme disease agent Borrelia burgdorferi which is critical to ensure infection after a tick b…

2013

Lyme disease is a tick-borne infection caused by the transmission of Borrelia burgdorferi from infected Ixodes ticks to a mammalian host during the blood meal. Previous studies have shown that the expression of B. burgdorferi surface-localized lipoproteins, which include BBA64, is up-regulated during the process of tick feeding. Although the exact function of BBA64 is not known, this lipoprotein is critical for the transmission of the spirochete from the tick salivary glands to the mammalian organism after a tick bite. Since the mechanism of development of the disease and the functions of the surface lipoproteins associated with borrel­iosis are still poorly understood, the crystal structur…

Models MolecularAntigens BacterialLyme DiseasebiologyIxodesTransmission (medicine)General MedicineTickbacterial infections and mycosesbiology.organism_classificationmedicine.diseaseMicrobiologyPathogenesisLyme diseaseX-Ray DiffractionStructural BiologyBorrelia burgdorferiSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationmedicineAnimalsIxodesBorrelia burgdorferiFunction (biology)LipoproteinActa crystallographica. Section D, Biological crystallography
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Fluorescent Small Molecule Probe to Modulate and Explore α2β1 Integrin Function

2011

Collagen binding integrins are an important family of cell surface receptors that mediate bidirectionally signals between the interior of the cell and the extracellular matrix. The protein-protein interactions between cells and collagen are necessary for many physiological functions, but also promote diseases. For example, the interaction of α2β1 integrin and collagen has been shown to have an important role in thrombus formation and cancer spread. The fact that the discovery of small molecules that can block such protein-protein interactions is highly challenging has significantly hindered the discovery of pharmaceutical agents to treat these diseases. Here, we present a rationally designe…

Models MolecularCellIntegrinBiochemistryCatalysisExtracellular matrixColloid and Surface ChemistryCell surface receptormedicineHumansta116Fluorescent DyesBinding SitesbiologyChemistryta1182General ChemistryFluorescenceSmall moleculeSpectrometry Fluorescencemedicine.anatomical_structureBiochemistryBiophysicsbiology.proteinCollagenα2β1 integrinIntegrin alpha2beta1Function (biology)Protein BindingJournal of the American Chemical Society
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Matrix Isolation and Ab Initio Study of Trans−Trans and Trans−Cis Dimers of Formic Acid

2010

Six trans-trans and five trans-cis dimeric structures of formic acid (HCOOH) are revealed by ab initio calculations. Four trans-trans and two trans-cis dimers are identified in the IR absorption spectra in argon matrices. The trans-cis dimers are obtained by narrow-band IR excitation of the vibrational transitions of the trans-trans dimers. Two trans-trans (tt3 and tt6) and one trans-cis (tc4) dimer are characterized experimentally for the first time. The tunneling decay rates of two trans-cis dimers (tc1 and tc4) are evaluated at different temperatures. A greater lifetime of the trans-cis dimers at elevated temperatures compared to the cis-monomer suggests that the high-energy conformers c…

Models MolecularFormatesSpectrophotometry InfraredFormic acidDimerMolecular ConformationAb initio010402 general chemistryPhotochemistry01 natural scienceschemistry.chemical_compoundAb initio quantum chemistry methods0103 physical sciencesPhysical and Theoretical ChemistryConformational isomerism010304 chemical physicsHydrogen bondMatrix isolationStereoisomerism0104 chemical sciences3. Good healthCrystallographychemistryQuantum TheoryThermodynamicsDimerizationCis–trans isomerismThe Journal of Physical Chemistry A
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Structure and Function of CutC Choline Lyase from Human Microbiota Bacterium Klebsiella pneumoniae.

2015

CutC choline trimethylamine-lyase is an anaerobic bacterial glycyl radical enzyme (GRE) that cleaves choline to produce trimethylamine (TMA) and acetaldehyde. In humans, TMA is produced exclusively by the intestinal microbiota, and its metabolite, trimethylamine oxide, has been associated with a higher risk of cardiovascular diseases. Therefore, information about the three-dimensional structures of TMA-producing enzymes is important for microbiota-targeted drug discovery. We have cloned, expressed, and purified the CutC GRE and the activating enzyme CutD from Klebsiella pneumoniae, a representative of the human microbiota. We have determined the first crystal structures of both the choline-…

Models MolecularKlebsiella pneumoniaeMetaboliteTrimethylamineLyasesmacromolecular substancesBiologydigestive systemBiochemistryMicrobiologyCholinechemistry.chemical_compoundBacterial ProteinsCatalytic DomainCholineChymotrypsinHumansMolecular Biologychemistry.chemical_classificationChymotrypsinMicrobiotaCell Biologybiology.organism_classificationLyaseEnzyme structureProtein Structure TertiaryKlebsiella pneumoniaeEnzymechemistryBiochemistrySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationProtein Structure and Foldingbiology.proteinChromatography GelElectrophoresis Polyacrylamide GelProtein MultimerizationThe Journal of biological chemistry
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Hydrogen-bond-mediated self-assembly of 26-membered diaza tetraester crowns of 3,5-disubstituted 1 h -pyrazole. Dimerization study in the solid state…

2011

By using an improved synthetic method reported earlier, the cyclic stannoxanes obtained from RN-diethanolamine (R = Me, Bu) and dibutyltin oxide have been reacted with 1H-pyrazole-3,5-dicarbonyl dichloride to afford 26-membered diaza tetraester crowns (1, R = Me; 3, R = Bu) and 39-membered triaza hexaester crowns (2, R = Me; 4, R = Bu). The new structures were identified from their analytical and spectroscopic (1H and 13C NMR, FAB-MS, and/or ESI-MS) data. Both diaza tetraester crowns (1 and 3), containing two 1H-pyrazole units, self-assemble into dimeric species through the formation of four hydrogen bonds involving the two NH pyrazole groups and the two tertiary amine groups of both crowns…

Models MolecularMagnetic Resonance SpectroscopyMolecular modelTertiary amineSolid-statePyrazoleCrystallography X-RayMedicinal chemistrychemistry.chemical_compoundOrganotin CompoundsAminesDibutyltin oxideHydrogen bondOrganic ChemistryEstersHydrogen BondingCarbon-13 NMRDeuteriumCrown CompoundsSolutionschemistryCyclizationEthanolaminesMolecular ProbesSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationPyrazolesChloroformSelf-assemblyDimerization
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Mapping the fluorophilicity of a hydrophobic pocket: synthesis and biological evaluation of tricyclic thrombin inhibitors directing fluorinated alkyl…

2006

In the completion of our fluorine scan of tricyclic inhibitors to map the fluorophilicity/fluorophobicity of the thrombin active site, a series of 11 new ligands featuring alkyl, alkenyl, and fluoroalkyl groups was prepared to explore fluorine effects on binding into the hydrophobic proximal (P) pocket, lined by Tyr 60A and Trp 60D, His 57, and Leu 99. The synthesis of the tricyclic scaffolds was based on the 1,3-dipolar cycloaddition of azomethine ylides, derived from L-proline and 4-bromobenzaldehyde, with N-(4-fluorobenzyl)maleimide. Introduction of alkyl, alkenyl, and partially fluorinated alkyl residues was achieved upon substitution of a sulfonyl group by mixed Mg/Zn organometallics f…

Models MolecularMagnetic Resonance SpectroscopySpectrophotometry InfraredStereochemistrySubstituentCrystallography X-RayBiochemistryAntithrombinschemistry.chemical_compoundDrug DiscoveryNon-covalent interactionsGeneral Pharmacology Toxicology and PharmaceuticsMaleimideAlkylPharmacologychemistry.chemical_classificationSulfonylNucleophilic additionbiologyMolecular StructureOrganic ChemistryActive siteFluorineCycloadditionchemistrySpectrometry Mass Matrix-Assisted Laser Desorption-Ionizationbiology.proteinMolecular MedicineChemMedChem
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A Fluorine Scan at the Catalytic Center of Thrombin: CF, COH, and COMe Bioisosterism and Fluorine Effects on pKa and logD Values

2006

A series of 16 tricyclic thrombin inhibitors was prepared by using the 1,3-dipolar cycloaddition of azomethine ylides derived from 3- or 4-hydroxyproline and 4-bromobenzaldehyde, with N-(4-fluorobenzyl)maleimide as the key step. The terminal pyrrolidine ring of the inhibitors was systematically substituted to explore the potential bioisosteric behavior of C-F, C-OH, and C-OMe residues pointing into the environment of the catalytic center of a serine protease. X-ray crystal structure analyses revealed a distinct puckering preference of this ring. Substitution by F, HO, and MeO has a strong effect on the basicity of the adjacent pyrrolidine nitrogen center which originates from two sigma-indu…

Models MolecularMagnetic Resonance SpectroscopyTertiary amineStereochemistrychemistry.chemical_elementCrystal structureBiochemistryPyrrolidinechemistry.chemical_compoundCatalytic DomainDrug DiscoveryNon-covalent interactionsGeneral Pharmacology Toxicology and PharmaceuticsMaleimidePharmacologychemistry.chemical_classificationMolecular StructureOrganic ChemistryThrombinFluorineAcceptorCycloadditionchemistrySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationFluorineMolecular MedicineChemMedChem
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News from an Ancient World: Two Novel Astacin Metalloproteases from the Horseshoe Crab

2008

In this work, we report the cloning, heterologous expression, and characterization of two novel astacin proteases from the chelicerate Limulus polyphemus (horseshoe crab), designated as LAST (Limulus astacin) and LAST_MAM (Limulus astacin containing a MAM domain), respectively. The expression pattern showed ubiquitous occurrence of LAST_MAM, while LAST was predominantly restricted to the eyes and brain, indicating a function in the nervous system. Both enzymes contain the characteristic metzincin-type zinc-binding region and Met turn. While LAST is made up only of the typical prodomain and astacin-like protease domain, LAST_MAM contains an additional MAM (meprin A5 protein tyrosine phosphat…

Models MolecularProteasesDNA ComplementaryInsectaProtein familymedicine.medical_treatmentMolecular Sequence DataContext (language use)Protein tyrosine phosphataseBiologyHydroxamic AcidsNervous SystemCollagen Type IGene Expression Regulation EnzymologicCell LineEvolution MolecularStructural BiologyHorseshoe CrabsmedicineAnimalsProtein oligomerizationAmino Acid SequenceRNA MessengerCloning MolecularMolecular BiologyPhylogenyExtracellular Matrix ProteinsProteaseBase SequenceCaseinsMetalloendopeptidasesbiology.organism_classificationProtein Structure TertiaryBiochemistryStructural Homology ProteinLimulusAstacinOligopeptidesProtein Processing Post-TranslationalJournal of Molecular Biology
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Sizzled Is Unique among Secreted Frizzled-related Proteins for Its Ability to Specifically Inhibit Bone Morphogenetic Protein-1 (BMP-1)/Tolloid-like …

2012

BMP-1/tolloid-like proteinases (BTPs) are major enzymes involved in extracellular matrix assembly and activation of bioactive molecules, both growth factors and anti-angiogenic molecules. Although the control of BTP activity by several enhancing molecules is well established, the possibility that regulation also occurs through endogenous inhibitors is still debated. Secreted frizzled-related proteins (sFRPs) have been studied as possible candidates, with highly contradictory results, after the demonstration that sizzled, a sFRP found in Xenopus and zebrafish, was a potent inhibitor of Xenopus and zebrafish tolloid-like proteases. In this study, we demonstrate that mammalian sFRP-1, -2, and …

Models MolecularProteasesFrizzledanimal structuresMolecular Sequence DataXenopusXenopus ProteinsBiochemistryBone morphogenetic protein 1Bone Morphogenetic Protein 1MiceXenopus laevismedicineAnimalsHumansProtease InhibitorsAmino Acid SequenceMolecular BiologyZebrafishGlycoproteinsSequence Homology Amino AcidbiologyExtracellular matrix assemblyfungiIntracellular Signaling Peptides and ProteinsTissue Inhibitor of MetalloproteinasesCell BiologySurface Plasmon Resonancebiology.organism_classificationMatrix MetalloproteinasesRecombinant ProteinsExtracellular MatrixWnt ProteinsBiochemistryMechanism of actionembryonic structuresEnzymologySignal transductionmedicine.symptomPeptide HydrolasesSignal TransductionJournal of Biological Chemistry
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The death-domain fold of the ASC PYRIN domain, presenting a basis for PYRIN/PYRIN recognition.

2003

The PYRIN domain is a conserved sequence motif identified in more than 20 human proteins with putative functions in apoptotic and inflammatory signalling pathways. The three-dimensional structure of the PYRIN domain from human ASC was determined by NMR spectroscopy. The structure determination reveals close structural similarity to death domains, death effector domains, and caspase activation and recruitment domains, although the structural alignment with these other members of the death-domain superfamily differs from previously predicted amino acid sequence alignments. Two highly positively and negatively charged surfaces in the PYRIN domain of ASC result in a strong electrostatic dipole …

Models MolecularProtein FoldingMagnetic Resonance SpectroscopyCARD Signaling Adaptor ProteinsProtein ConformationProtein domainMolecular Sequence DataStatic ElectricityBiologyPyrin domainProtein Structure SecondaryConserved sequenceProtein structureStructural BiologyAnimalsHumansAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequenceZebrafishDeath domainGeneticsModels StatisticalSequence Homology Amino AcidProteinsPyrinZebrafish ProteinsCell biologyProtein Structure TertiaryCARD Signaling Adaptor ProteinsCytoskeletal ProteinsSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationProtein foldingProtein BindingSignal TransductionJournal of molecular biology
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