Search results for "Structural Biology."

showing 10 items of 822 documents

The regulation mechanism for the auto-inhibition of binding of human filamin A to integrin.

2009

The ability of adhesion receptors to transmit biochemical signals and mechanical force across cell membranes depends on interactions with the actin cytoskeleton. Human filamins are large actin cross-linking proteins that connect integrins to the cytoskeleton. Filamin binding to the cytoplasmic tail of beta integrins has been shown to prevent integrin activation in cells, which is important for controlling cell adhesion and migration. The molecular-level mechanism for filamin binding to integrin has been unclear, however, as it was recently demonstrated that filamin undergoes intramolecular auto-inhibition of integrin binding. In this study, using steered molecular dynamics simulations, we f…

Models MolecularProtein Foldinganimal structuresIntegrin beta ChainsFilaminsmacromolecular substancesBiologyFilaminCD49cCollagen receptorFilamin bindingPhosphoserineContractile ProteinsStructural BiologyHumansPhosphorylationMolecular BiologyIntegrin bindingBinding SitesMicrofilament ProteinsActin cytoskeletonCell biologybody regionsIntegrin alpha Mbiology.proteinIntegrin beta 6Stress MechanicalPeptidesProtein BindingJournal of molecular biology
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Quality assessment of protein NMR structures.

2013

Biomolecular NMR structures are now routinely used in biology, chemistry, and bioinformatics. Methods and metrics for assessing the accuracy and precision of protein NMR structures are beginning to be standardized across the biological NMR community. These include both knowledge-based assessment metrics, parameterized from the database of protein structures, and model versus data assessment metrics. On line servers are available that provide comprehensive protein structure quality assessment reports, and efforts are in progress by the world-wide Protein Data Bank (wwPDB) to develop a biomolecular NMR structure quality assessment pipeline as part of the structure deposition process. These qu…

Models MolecularProtein structure; NMR spectroscopyMagnetic Resonance SpectroscopyProtein ConformationAnalytical chemistryBiology010402 general chemistrycomputer.software_genre01 natural sciencesArticle03 medical and health sciencesStructural BiologyServerDatabases ProteinMolecular BiologyNuclear Magnetic Resonance Biomolecular030304 developmental biology0303 health sciencesExtramuralQuality assessmentData assessmentResearchProteinsReproducibility of ResultsNuclear magnetic resonance spectroscopycomputer.file_formatProtein Data Bank0104 chemical sciencesData miningcomputerDeposition processCurrent opinion in structural biology
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Kinetics of proton release and uptake by channelrhodopsin-2

2012

Electrophysiological experiments showed that the light-activated cation channel channelrhodopsin-2 (ChR2) pumps protons in the absence of a membrane potential. We determined here the kinetics of transient pH change using a water-soluble pH-indicator. It is shown that ChR2 released protons prior to uptake with a stoichiometry of 0.3 protons per ChR2. Comparison to the photocycle kinetics revealed that proton release and uptake match rise and decay of the View the MathML sourceP3520 intermediate. As the View the MathML sourceP3520 state also represents the conductive state of cation channeling, the concurrence of proton pumping and channel gating implies an intimate mechanistic link of the tw…

Models MolecularRhodopsinProtonKineticsBiophysicsAnalytical chemistryChannelrhodopsinBacteriorhodopsinBiochemistry530Protein Structure SecondaryProton transferStructural BiologyGeneticsMolecular BiologyIon channelMembrane potentialbiologyChemistryfungiBacteriorhodopsinBiological TransportCell BiologyHydrogen-Ion ConcentrationProton PumpsOptogeneticsKineticsRhodopsinBiophysicsbiology.proteinProtonsIon channelStoichiometry
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Structural Characterization of Set1 RNA Recognition Motifs and their Role in Histone H3 Lysine 4 Methylation

2006

Departament de Bioquimica iBiologia Molecular, Universitatde Valencia, C/Dr Moliner 50,46100, Burjassot, SpainThe yeast Set1 histone H3 lysine 4 (H3K4) methyltransferase contains, inaddition to its catalytic SET domain, a conserved RNA recognition motif(RRM1). We present here the crystal structure and the secondary structureassignment in solution of the Set1 RRM1. Although RRM1 has the expectedβαββαβ RRM-fold, it lacks the typical RNA-binding features of thesemodules. RRM1 is not able to bind RNA by itself in vitro, but a constructcombining RRM1 with a newly identified downstream RRM2 specificallybinds RNA. Invivo,H3K4 methylation isnot affectedbyapoint mutation inRRM2 that preserves Set1 s…

Models MolecularRiboswitchHistone H3 Lysine 4Saccharomyces cerevisiae ProteinsRNA-induced transcriptional silencingSurface Properties[SDV]Life Sciences [q-bio]Molecular Sequence DataSaccharomyces cerevisiae[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]BiologyMethylationHistonesStructure-Activity Relationship03 medical and health sciencesStructural BiologyHistone methylation[SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Amino Acid SequenceProtein Structure QuaternaryMolecular BiologyConserved Sequence030304 developmental biology0303 health sciencesRNA recognition motifLysine030302 biochemistry & molecular biologyRNARNA FungalHistone-Lysine N-MethyltransferaseNon-coding RNAMolecular biology[SDV] Life Sciences [q-bio]DNA-Binding ProteinsProtein SubunitsBiochemistryHistone methyltransferaseSequence AlignmentProtein BindingTranscription Factors
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Antibody inhibition of the transcriptase activity of the rotavirus DLP: a structural view.

2001

On entering the host cell the rotavirus virion loses its outer shell to become a double-layered particle (DLP). The DLP then transcribes the 11 segments of its dsRNA genome using its own transcriptase complex, and the mature mRNA emerges along the 5-fold axis. In order to better understand the transcription mechanism and the role of VP6 in transcription we have studied three monoclonal antibodies against VP6: RV-238 which inhibits the transcriptase activity of the DLP; and RV-133 and RV-138 which have no effect on transcription. The structures obtained by cryo-electron microscopy of the DLP/Fab complexes and by X-ray crystallography of the VP6 trimer and the VP6/Fab-238 complex have been co…

Models MolecularRotavirusConformational changeSTRUCTUREMature messenger RNAmedicine.drug_classProtein ConformationvirusesBiologyMonoclonal antibodyAntibodies ViralCrystallography X-RayEpitope03 medical and health sciencesEpitopesImmunoglobulin Fab FragmentsCapsidStructural BiologyTranscription (biology)medicine[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyCRISTALLOGRAPHIE[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyRNA MessengerMolecular BiologyAntigens Viral030304 developmental biology0303 health sciencesMessenger RNA030302 biochemistry & molecular biologyCryoelectron Microscopyvirus diseasesRNADNA-Directed RNA PolymerasesMolecular biologyReverse transcriptase3. Good healthVIROLOGIECapsid ProteinsJournal of molecular biology
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Structures of yeast peroxisomal Δ(3),Δ(2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks f…

2015

Δ3,Δ2-Enoyl-CoA isomerases (ECIs) catalyze the shift of a double bond from 3Z- or 3E-enoyl-CoA to 2E-enoyl-CoA. ECIs are members of the crotonase superfamily. The crotonase framework is used by many enzymes to catalyze a wide range of reactions on acyl-CoA thioesters. The thioester O atom is bound in a conserved oxyanion hole. Here, the mode of binding of acyl-CoA substrate analogues to peroxisomalSaccharomyces cerevisiaeECI (ScECI2) is described. The best defined part of the bound acyl-CoA molecules is the 3′,5′-diphosphate-adenosine moiety, which interacts with residues of loop 1 and loop 2, whereas the pantetheine part is the least well defined. The catalytic base, Glu158, is hydrogen-bo…

Models MolecularSaccharomyces cerevisiae ProteinsDouble bondStereochemistryProtein ConformationIsomeraseSaccharomyces cerevisiaeEnoyl CoA isomeraseThioesterPhotochemistryDodecenoyl-CoA Isomerasebeta-oxidationSubstrate SpecificityStructural Biologyddc:570Catalytic DomainEnzyme StabilitySide chainMoietyta116chemistry.chemical_classificationHydrogen bondenoyl-CoA isomeraseta1182Hydrogen BondingGeneral Medicinehydrogen-bond networkcrotonaseoxyanion holechemistryAcyl Coenzyme AOxyanion holeOxidation-ReductionProtein BindingActa crystallographica. Section D, Biological crystallography
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Structure-based analyses of Salmonella RcsB variants unravel new features of the Rcs regulon

2021

18 páginas, 7 figuras, 2 tablas

Models MolecularSalmonella typhimuriumIdentificationSignaling SystemTranscription GeneticTranscription FactorAcademicSubjects/SCI00010Protein ConformationProtein Data Bank (RCSB PDB)ExpressionBiologymedicine.disease_causeRegulonBiofilm Formation03 medical and health sciencesBacterial ProteinsCapsule SynthesisStructural BiologyGeneticsmedicineTranscriptional regulationPhosphorylationPromoter Regions GeneticTranscription factorGene030304 developmental biologyRegulation of gene expression0303 health sciencesMutationBinding Sites030306 microbiologyPromoterGene Expression Regulation BacterialBiología y Biomedicina / BiologíaRepressionCell biologyRegulonEscherichia-Coli K-12MutationGenome BacterialPhosphorelay SystemNucleic Acids Research
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On the molecular structure of human neuroserpin polymers

2012

The polymerization of serpins is at the root of a large class of diseases; the molecular structure of serpin polymers has been recently debated. In this work, we study the polymerization kinetics of human neuroserpin by Fourier Transform Infra Red spectroscopy and by time-lapse Size Exclusion Chromatography. First, we show that two distinct neuroserpin polymers, formed at 45 and 85°C, display the same isosbestic points in the Amide I' band, and therefore share common secondary structure features. We also find a concentration independent polymerization rate at 45°C suggesting that the polymerization rate-limiting step is the formation of an activated monomeric species. The polymer structures…

Models MolecularSize-exclusion chromatographySerpinBiochemistryProtein Structure Secondaryserpinopathieprotein aggregationchemistry.chemical_compoundStructural BiologyNeuroserpinCatalytic DomainSpectroscopy Fourier Transform InfraredPolymer chemistryHumansMolecular BiologyProtein secondary structureSerpinschemistry.chemical_classificationIsosbestic pointChemistryNeuropeptidesserpinPolymerSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)KineticsCrystallographyMonomerprotein aggregation; serpins; serpinopathies; serpin polymerization; FTIRPolymerizationFTIRChromatography GelProtein Multimerizationserpin polymerization
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Alkali metal mediated resorcarene capsules: An ESI-FTICRMS study on gas-phase structure and cation binding of tetraethyl resorcarene and its per-meth…

2002

AbstractElectrospray ionization Fourier transform ion cyclotron resonance mass spectrometry (ESI-FTICRMS) with additional ab initio calculations were used to examine the alkali metal cation binding selectivity (i.e., molecular recognition) and host properties of tetraethyl resorcarene (1) and its per-methylated derivative (2). The significance of intramolecular hydrogen bonding for the crown conformation was demonstrated. The presence of intramolecular flip-flop hydrogen bonding in 1 was confirmed both with calculations and in ND3-exchange experiments. All the alkali metal cations formed host–guest complexes by docking inside the cavity of the host. Complexation with the larger cations, esp…

Models MolecularSpectrometry Mass Electrospray IonizationCation bindingFourier AnalysisHydrogen bondChemistryStereochemistryElectrospray ionizationMolecular ConformationHydrogen BondingAlkaliesIon cyclotron resonance spectrometryMethylationFourier transform ion cyclotron resonanceMolecular recognitionMetalsStructural BiologyIntramolecular forcePolymer chemistryMoleculePolycyclic CompoundsSpectroscopyJournal of the American Society for Mass Spectrometry
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Effect of protonation and deprotonation on the gas phase reactivity of fluorinated 1,2,4-triazines

2008

Positive and negative electrospray mass spectrometry (MS), in-time and in-space MS n experiments, high-resolution and accurate mass measurements obtained with an Orbitrap, together with density functional theory calculations have been used to study the gas-phase ion chemistry of a series of fluorinated 1,2,4-triazines. As a result of low-energy collision-induced dissociations, occurring in an ion trap and in a triple quadrupole, their protonated and deprotonated molecules show interesting features depending on the nature and structure of the precursor ions. The occurrence of elimination/hydration reactions produced by positive ions in the ion trap is noteworthy. Decompositions of deprotonat…

Models MolecularSpectrometry Mass Electrospray IonizationIONIZATION MASS-SPECTROMETRYFluorine CompoundsAnalytical chemistryProtonationTandem mass spectrometryPhotochemistryOrbitrapIonlaw.inventionchemistry.chemical_compoundDeprotonationStructural BiologylawCHEMISTRYMoleculeComputer SimulationPhysics::Chemical PhysicsNEGATIVE ELECTROSPRAY-IONIZATIONCOLLISION-INDUCED DISSOCIATIONSpectroscopyTRIAZINESHYDRAZINEchemistryModels ChemicalHydroxyl radicalIon trapProtonsFRAGMENTATIONHETEROCYCLES
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