Search results for "cysteine"

showing 10 items of 550 documents

In Silico Insights into the SARS CoV-2 Main Protease Suggest NADH Endogenous Defences in the Control of the Pandemic Coronavirus Infection

2020

COVID-19 is a pandemic health emergency faced by the entire world. The clinical treatment of the severe acute respiratory syndrome (SARS) CoV-2 is currently based on the experimental administration of HIV antiviral drugs, such as lopinavir, ritonavir, and remdesivir (a nucleotide analogue used for Ebola infection). This work proposes a repurposing process using a database containing approximately 8000 known drugs in synergy structure- and ligand-based studies by means of the molecular docking and descriptor-based protocol. The proposed in silico findings identified new potential SARS CoV-2 main protease (MPRO) inhibitors that fit in the catalytic binding site of SARS CoV-2 MPRO. Several sel…

Models Molecular0301 basic medicineAgingmedicine.medical_treatmentcoronaviruslcsh:QR1-502Viral Nonstructural Proteinsmedicine.disease_causelcsh:Microbiology0302 clinical medicineSettore BIO/10 - BiochimicaCoronavirus 3C ProteasesCoronavirusvirus diseasesLopinavirHypothesisMolecular Docking SimulationCysteine EndopeptidasesDrug repositioningInfectious Diseases030220 oncology & carcinogenesisCoronavirus InfectionsOxidation-Reductionmedicine.drugDNA damageIn silicoPneumonia ViralBiologyAntiviral AgentsHIV-proteaseBetacoronavirus03 medical and health sciencesSARS-CoV-2 main proteaseVirologymedicineHumansComputer SimulationProtease InhibitorsPandemicsBinding SitesProteaseSARS-CoV-2Drug RepositioningCOVID-19HIV Protease InhibitorsDRUDIT web servicemolecular dockingNADbiology.organism_classificationVirologySettore CHIM/08 - Chimica FarmaceuticaCOVID-19 Drug Treatmentcoronaviru030104 developmental biologyNADHRitonavirBetacoronavirusDNA Damage
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Changes in the hydrogen-bonding strength of internal water molecules and cysteine residues in the conductive state of channelrhodopsin-1

2014

Water plays an essential role in the structure and function of proteins, particularly in the less understood class of membrane proteins. As the first of its kind, channelrhodopsin is a light-gated cation channel and paved the way for the new and vibrant field of optogenetics, where nerve cells are activated by light. Still, the molecular mechanism of channelrhodopsin is not understood. Here, we applied time-resolved FT-IR difference spectroscopy to channelrhodopsin-1 from Chlamydomonas augustae. It is shown that the (conductive) P2(380) intermediate decays with τ ≈ 40 ms and 200 ms after pulsed excitation. The vibrational changes between the closed and the conductive states were analyzed in…

Models Molecular570StereochemistryGeneral Physics and AstronomyInfrared spectroscopy530Ion Channelschemistry.chemical_compoundAmideRhodopsins MicrobialSpectroscopy Fourier Transform InfraredSide chainMoleculePeptide bondCysteinePhysical and Theoretical ChemistryPlant Proteinschemistry.chemical_classificationHydrogen bondChlamydomonasWaterFísicaHydrogen BondingQuímicaCrystallographychemistryThiolProteïnesCysteineThe Journal of Chemical Physics
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A bioinformatical approach suggests the function of the autoimmune hepatitis target antigen soluble liver antigen/liver pancreas

2001

Antibodies to a soluble liver antigen/liver pancreas (SLA/LP) appear to be highly specific for the diagnosis of autoimmune hepatitis. The SLA/LP target antigen was recently identified as a hitherto unknown gene encoding 474 amino acid residues. The function of this antigen remains unclear, because it does not share sequence homology with proteins of known function stored in any of the publicly accessible databases. Therefore we used a new theoretical method called fold recognition and could show that the SLA/LP sequence is compatible with the architecture of the superfamily of pyridoxal phosphate (PLP; vitamin B6)-dependent transferases. Its function is likely to be that of a serine hydroxy…

Models MolecularAutoimmune diseaseHepatitisHepatologySelenocysteineMolecular Sequence DataComputational BiologyAutoimmune hepatitisBiologymedicine.diseaseAutoantigensHepatitis Autoimmunechemistry.chemical_compoundchemistryBiochemistryAntigenSerine hydroxymethyltransferasebiology.proteinmedicineHumansAmino Acid SequenceAntibodyPyridoxal phosphateHepatology
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Functional cysteine-less subunits of the transporter associated with antigen processing (TAP1 and TAP2) by de novo gene assembly

2002

AbstractWithin the adaptive immune system the transporter associated with antigen processing (TAP) plays a pivotal role in loading of peptides onto major histocompatibility (MHC) class I molecules. As a central tool to investigate the structure and function of the TAP complex, we created cysteine-less human TAP subunits by de novo gene synthesis, replacing all 19 cysteines in TAP1 and TAP2. After expression in TAP-deficient human fibroblasts, cysteine-less TAP1 and TAP2 are functional with respect to adenosine triphosphate (ATP)-dependent peptide transport and inhibition by ICP47 from herpes simplex virus. Cysteine-less TAP1 and TAP2 restore maturation and intracellular trafficking of MHC c…

Models MolecularBiophysicsBiological Transport ActiveBiologyMajor histocompatibility complexTransfectionBiochemistryCell Linechemistry.chemical_compoundAdenosine TriphosphateStructural BiologyATP Binding Cassette Transporter Subfamily B Member 3Cysteine-scanning mutagenesisMHC class IGeneticsHumansCysteineATP Binding Cassette Transporter Subfamily B Member 2Molecular BiologyAntigen PresentationAntigen processingHistocompatibility Antigens Class ICell BiologyTransporter associated with antigen processingMolecular biologyRecombinant ProteinsCell biologyProtein SubunitschemistryAmino Acid SubstitutionAntigen processingPeptide transportMembrane proteinbiology.proteinAdenosine triphosphate-binding cassette transporterTAP2ATP-Binding Cassette TransportersTAP1Adenosine triphosphateFEBS Letters
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Diversity of Omega Glutathione Transferases in mushroom-forming fungi revealed by phylogenetic, transcriptomic, biochemical and structural approaches

2021

International audience; The Omega class of glutathione transferases (GSTs) forms a distinct class within the cytosolic GST superfamily because most of them possess a catalytic cysteine residue. The human GST Omega 1 isoform was first characterized twenty years ago, but it took years of work to clarify the roles of the human isoforms. Concerning the kingdom of fungi, little is known about the cellular functions of Omega glutathione transferases (GSTOs), although they are widely represented in some of these organisms. In this study, we re-assess the phylogeny and the classification of GSTOs based on 240 genomes of mushroom-forming fungi (Agaricomycetes). We observe that the number of GSTOs is…

Models MolecularGene isoformProtein ConformationCrystallography X-RayMicrobiologyAgaricomycetesstructure-functionFungal ProteinsSerine03 medical and health scienceschemistry.chemical_compoundPhylogeneticsGeneticsPolyporalesflavonoid[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyglutathionePhylogeny[SDV.MP.MYC]Life Sciences [q-bio]/Microbiology and Parasitology/MycologyGlutathione Transferase030304 developmental biologychemistry.chemical_classification0303 health sciencesBinding Sitesbiology030306 microbiologyGene Expression ProfilingGenetic VariationGlutathionebiology.organism_classificationenzymeEnzymeBiochemistrychemistryfungi[SDE.BE]Environmental Sciences/Biodiversity and EcologyAgaricalesCysteine[SDV.EE.IEO]Life Sciences [q-bio]/Ecology environment/Symbiosis
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Mitochondrially encoded cysteine predicts animal lifespan

2007

Summary The role of genetic factors in the determination of lifespan is undisputed. However, numerous successful efforts to identify individual genetic modulators of longevity have not yielded yet a quantitative measure to estimate the lifespan of a species from scratch, merely based on its genomic constitution. Here, we report on a meta-examination of genome sequences from 248 animal species with known maximum lifespan, including mammals, birds, fish, insects, and helminths. Our analysis reveals that the frequency with which cysteine is encoded by mitochondrial DNA is a specific and phylogenetically ubiquitous molecular indicator of aerobic longevity: long-lived species synthesize respirat…

Models MolecularGeneticsAgingMitochondrial DNAFree Radicalsmedia_common.quotation_subjectLongevityRespiratory chainLongevityComputational BiologyLocus (genetics)Cell BiologyMitochondrionBiologyProtein oxidationDNA MitochondrialGenomeMitochondriaMitochondrial ProteinsAnimalsHumansCysteineAnaerobic bacteriaPhylogenymedia_commonAging Cell
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Optimization of Triazine Nitriles as Rhodesain Inhibitors: Structure-Activity Relationships, Bioisosteric Imidazopyridine Nitriles, and X-ray Crystal…

2013

The cysteine protease rhodesain of Trypanosoma brucei parasites causing African sleeping sickness has emerged as a target for the development of new drug candidates. Based on a triazine nitrile moiety as electrophilic headgroup, optimization studies on the substituents for the S1, S2, and S3 pockets of the enzyme were performed using structure-based design and resulted in inhibitors with inhibition constants in the single-digit nanomolar range. Comprehensive structure-activity relationships clarified the binding preferences of the individual pockets of the active site. The S1 pocket tolerates various substituents with a preference for flexible and basic side chains. Variation of the S2 subs…

Models MolecularImidazopyridineMolecular modelNitrilePyridinesStereochemistryCathepsin LTrypanosoma brucei bruceiSubstituentCysteine Proteinase InhibitorsCrystallography X-RayLigandsBiochemistryStructure-Activity Relationshipchemistry.chemical_compoundParasitic Sensitivity TestsNitrilesDrug DiscoveryHumansMoietyGeneral Pharmacology Toxicology and PharmaceuticsTriazinePharmacologyDose-Response Relationship DrugMolecular StructurebiologyTriazinesChemistryLigandOrganic ChemistryImidazolesActive siteCysteine Endopeptidasesbiology.proteinMolecular MedicineChemMedChem
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Site-specific Labelling with a Metal Chelator for Protein-structure Refinement

2004

A single free Cys sidechain in the N-terminal domain of the E. coli arginine repressor was covalently derivatized with S-cysteaminyl-EDTA for site-specific attachment of paramagnetic metal ions. The effects of chelated metal ions were monitored with (15)N-HSQC spectra. Complexation of Co(2+), which has a fast relaxing electron spin, resulted in significant pseudocontact shifts, but also in peak doubling which was attributed to the possibility of forming two different stereoisomers of the EDTA-Co(2+) complex. In contrast, complexation of Cu(2+) or Mn(2+), which have slowly relaxing electron spins, did not produce chemical shift changes and yielded self-consistent sets of paramagnetic relaxat…

Models MolecularMagnetic Resonance SpectroscopyTime FactorsMetal ions in aqueous solutionElectronsGadoliniumBiochemistryIonParamagnetismchemistry.chemical_compoundNuclear magnetic resonanceBacterial ProteinsAmideEscherichia coliChelationCysteineEdetic AcidSpectroscopyChelating AgentsIonsManganeseElectronic correlationChemistryRelaxation (NMR)Electron Spin Resonance SpectroscopyProteinsCobaltDNAProtein Structure TertiaryRepressor ProteinsCrystallographyModels ChemicalCovalent bondProtonsCopperJournal of Biomolecular NMR
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Pore formation by Vibrio cholerae cytolysin follows the same archetypical mode as beta-barrel toxins from gram-positive organisms.

2009

Vibrio cholerae cytolysin (VCC) forms SDS-stable heptameric beta-barrel transmembrane pores in mammalian cell membranes. In contrast to structurally related pore formers of gram-positive organisms, no oligomeric prepore stage of assembly has been detected to date. In the present study, disulfide bonds were engineered to tie the pore-forming amino acid sequence to adjacent domains. In their nonreduced form, mutants were able to bind to rabbit erythrocytes and to native erythrocyte membranes suspended in PBS solution and form SDS-labile oligomers. These remained nonfunctional and represented the long-sought VCC prepores. Disulfide bond reduction in these oligomers released the pore-forming se…

Models MolecularPore Forming Cytotoxic ProteinsMutantBiologyIn Vitro Techniquesmedicine.disease_causeGram-Positive BacteriaBiochemistryModels Biologicalchemistry.chemical_compoundProtein structureGeneticsmedicineAnimalsCysteineProtein Structure QuaternaryMolecular BiologyPeptide sequenceVibrio choleraeCytotoxinsErythrocyte MembraneTransmembrane proteinRecombinant ProteinsMonomerMembraneBiochemistrychemistryVibrio choleraeMutagenesis Site-DirectedCytolysinRabbitsBiotechnologyFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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Tuning and Predicting Biological Affinity: Aryl Nitriles as Cysteine Protease Inhibitors

2012

A series of aryl nitrile-based ligands were prepared to investigate the effect of their electrophilicity on the affinity against the cysteine proteases rhodesain and human cathepsin L. Density functional theory calculations provided relative reactivities of the nitriles, enabling prediction of their biological affinity and cytotoxicity and a clear structure-activity relationship.

Models MolecularProteasesNitrileCathepsin LTrypanosoma brucei bruceiCysteine Proteinase InhibitorsBiochemistryCysteine Proteinase InhibitorsCathepsin Lchemistry.chemical_compoundCatalytic DomainNitrilesHumansOrganic chemistryPhysical and Theoretical ChemistryCathepsinbiologyArylOrganic ChemistryCombinatorial chemistryCysteine proteaseCysteine EndopeptidaseschemistryDrug Designbiology.proteinCysteineOrg. Biomol. Chem.
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