Search results for "serine"

showing 10 items of 590 documents

Construction of a dual chain pseudotetrameric chicken avidin by combining two circularly permuted avidins.

2004

Two distinct circularly permuted forms of chicken avidin were designed with the aim of constructing a fusion avidin containing two biotin-binding sites in one polypeptide. The old N and C termini of wild-type avidin were connected to each other via a glycine/serine-rich linker, and the new termini were introduced into two different loops. This enabled the creation of the desired fusion construct using a short linker peptide between the two different circularly permuted subunits. The circularly permuted avidins (circularly permuted avidin 5 → 4 and circularly permuted avidin 6 → 5) and their fusion, pseudotetrameric dual chain avidin, were biologically active, i.e. showed biotin binding, and…

Models MolecularBiotin bindingProtein DenaturationProtein FoldingStereochemistryProtein ConformationProtein subunitMolecular Sequence DataGlycineBiotinBiochemistrySensitivity and SpecificityProtein Structure Secondarystomatognathic systemChain (algebraic topology)SerineAnimalsAmino Acid SequenceBinding siteProtein Structure QuaternaryMolecular BiologyLinker peptideBinding SitesbiologyCell Biologyrespiratory systemAvidinProtein Structure TertiaryCrystallographyKineticsMutationbiology.proteinChromatography GelElectrophoresis Polyacrylamide GelEndopeptidase KPeptidesLinkerChickensAvidinProtein BindingThe Journal of biological chemistry
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Activation of EDTA-resistant Gelatinases in Malignant Human Tumors

2006

Abstract Among the many proteases associated with human cancer, seprase or fibroblast activation protein α, a type II transmembrane glycoprotein, has two types of EDTA-resistant protease activities: dipeptidyl peptidase and a 170-kDa gelatinase activity. To test if activation of gelatinases associated with seprase could be involved in malignant tumors, we used a mammalian expression system to generate a soluble recombinant seprase (r-seprase). In the presence of putative EDTA-sensitive activators, r-seprase was converted into 70- to 50-kDa shortened forms of seprase (s-seprase), which exhibited a 7-fold increase in gelatinase activity, whereas levels of dipeptidyl peptidase activity remaine…

Models MolecularCancer ResearchProteasesProtein ConformationDipeptidyl-peptidase activityIn situ hybridizationBiologyDipeptidyl peptidaseArticleCell LineFibroblast activation protein alphaNeoplasmsEndopeptidasesmedicineGelatinaseAnimalsHumansDipeptidyl-Peptidases and Tripeptidyl-PeptidasesEdetic AcidSerine EndopeptidasesMembrane ProteinsHaplorhinimedicine.diseaseRecombinant Proteinsseprase fibroblast activation protein alpha (FAP-α) gelatinase activation malignant tumorEnzyme ActivationOncologyBiochemistryGelatinasesCancer researchImmunohistochemistryAdenocarcinoma
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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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A Ser residue influences the structure and stability of a Pro-kinked transmembrane helix dimer

2012

AbstractWhen localized adjacent to a Pro-kink, Thr and Ser residues can form hydrogen bonds between their polar hydroxyl group and a backbone carbonyl oxygen and thereby modulate the actual bending angle of a distorted transmembrane α-helix. We have used the homo-dimeric transmembrane cytochrome b559′ to analyze the potential role of a highly conserved Ser residue for assembly and stabilization of transmembrane proteins. Mutation of the conserved Ser residue to Ala resulted in altered heme binding properties and in increased stability of the holo-protein, most likely by tolerating subtle structural rearrangements upon heme binding. The results suggest a crucial impact of an intrahelical Ser…

Models MolecularProlineHeme bindingStereochemistryDimerMolecular ConformationBiophysicsCofactor bindingHemeBiochemistryProtein Structure Secondarychemistry.chemical_compoundProtein structureProtein stabilitySerineProtein foldingCofactor bindingHydrogen bondCell MembranePhotosystem II Protein ComplexHydrogen BondingCell BiologyCytochrome b GroupTransmembrane proteinProtein Structure TertiaryOxygenTransmembrane domainHelix interactionchemistrySpectrophotometryMembrane proteinMutationTransmembrane helixProtein foldingDimerizationProtein BindingBiochimica et Biophysica Acta (BBA) - Biomembranes
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Flavonoids as noncompetitive inhibitors of Dengue virus NS2B-NS3 protease: Inhibition kinetics and docking studies

2014

NS2B-NS3 is a serine protease of the Dengue virus considered a key target in the search for new antiviral drugs. In this study flavonoids were found to be inhibitors of NS2B-NS3 proteases of the Dengue virus serotypes 2 and 3 with IC50 values ranging from 15 to 44 μM. Agathisflavone (1) and myricetin (4) turned out to be noncompetitive inhibitors of dengue virus serotype 2 NS2B-NS3 protease with Ki values of 11 and 4.7 μM, respectively. Docking studies propose a binding mode of the flavonoids in a specific allosteric binding site of the enzyme. Analysis of biomolecular interactions of quercetin (5) with NT647-NHS-labeled Dengue virus serotype 3 NS2B-NS3 protease by microscale thermophoresis…

Models MolecularProteasesSerine Proteinase Inhibitorsvirusesmedicine.medical_treatmentClinical BiochemistryPharmaceutical ScienceDengue virusmedicine.disease_causeAntiviral AgentsBiochemistryStructure-Activity Relationshipchemistry.chemical_compoundDrug DiscoverymedicineMolecular BiologyFlavonoidsSerine proteaseNS3ProteasebiologyMicroscale thermophoresisSerine EndopeptidasesOrganic ChemistryDengue VirusVirologyMolecular Docking SimulationKineticschemistryBiochemistryDocking (molecular)biology.proteinMolecular MedicineMyricetinBioorganic & Medicinal Chemistry
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The Parkinson Disease Gene LRRK2: Evolutionary and Structural Insights

2006

Mutations in the human leucine-rich repeat kinase 2 (LRRK2) gene are associated with both familial and sporadic Parkinson disease (PD). LRRK2 belongs to a gene family known as Roco. Roco genes encode for large proteins with several protein domains. Particularly, all Roco proteins have a characteristic GTPase domain, named Roc, plus a domain of unknown function called COR. In addition, LRRK2 and several other Roco proteins also contain a protein kinase domain. In this study, I use a combination of phylogenetic and structural analyses of the COR, Roc, and kinase domains present in Roco proteins to describe the origin and evolutionary history of LRRK2. Phylogenetic analyses using these domains…

Models MolecularProtein ConformationMolecular Sequence DataProtein domainGTPaseProtein Serine-Threonine KinasesBiologyLeucine-Rich Repeat Serine-Threonine Protein Kinase-2MAP3K7SH3 domainGTP PhosphohydrolasesEvolution MolecularGeneticsAnimalsHumansDictyosteliumAmino Acid Sequencec-RafMolecular BiologyPhylogenyEcology Evolution Behavior and SystematicsGeneticsSequence Homology Amino AcidParkinson DiseaseLRRK2Protein Structure Tertiarynervous system diseasesDisease Models AnimalProtein kinase domainRabProtein KinasesMolecular Biology and Evolution
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Cis autocatalytic cleavage of glycine-linked Zika virus NS2B-NS3 protease constructs.

2019

The flaviviral heterodimeric serine protease NS2B-NS3, consisting of the NS3 protease domain and the NS2B co-factor, is essential for ZIKA virus maturation and replication in cells. For in vitro studies a 'linked' construct, where a polyglycine linker connects NS2BCF and NS3pro , is often used. This construct undergoes autocatalytic cleavage. Here, we show that linked ZIKV NS2BCF -NS3pro is cleaved in cis in the NS2BCF exclusively at position R95 and not at the previously proposed alternate cleavage site at residue R29 in the NS3pro . Cleavage neither affects protease stability nor activity, despite some observed differences in spectroscopic behavior. This minimally modified construct may t…

Models MolecularProtein Conformationmedicine.medical_treatmentBiophysicsViral Nonstructural ProteinsCleavage (embryo)ArginineVirus ReplicationBiochemistryCatalysisZika virus03 medical and health sciencesViral ProteinsStructural BiologyGeneticsmedicineHomeostasisMolecular Biology030304 developmental biologySerine protease0303 health sciencesNS3ProteasebiologyChemistryCircular Dichroism030302 biochemistry & molecular biologySerine EndopeptidasesCell BiologyZika Virusbiology.organism_classificationIn vitroRecombinant ProteinsFlavivirusSpectrometry FluorescenceBiochemistrybiology.proteinProtein MultimerizationPeptidesLinkerPeptide HydrolasesFEBS lettersReferences
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The NS3/4A proteinase of the hepatitis C virus: unravelling structure and function of an unusual enzyme and a prime target for antiviral therapy

1999

The hepatitis C virus (HCV) is a major causative agent of transfusion-acquired and sporadic non-A, non-B hepatitis worldwide. Infections most often persist and lead, in approximately 50% of all patients, to chronic liver disease. As is characteristic for a member of the family Flaviviridae, HCV has a plus-strand RNA genome encoding a polyprotein, which is cleaved co- and post-translationally into at least 10 different products. These cleavages are mediated, among others, by a virally encoded chymotrypsin-like serine proteinase located in the N-terminal domain of non-structural protein 3 (NS3). Activity of this enzyme requires NS4A, a 54-residue polyprotein cleavage product, to form a stable…

Models MolecularProtein ConformationvirusesHepatitis C virusMolecular Sequence DataHepacivirusViral Nonstructural ProteinsBiologymedicine.disease_causeAntiviral AgentsSerineProtein structureVirologymedicineProtease InhibitorsAmino Acid SequenceHepatitischemistry.chemical_classificationNS3HepatologySerine EndopeptidasesRNAmedicine.diseaseVirologyNS2-3 proteaseInfectious DiseasesEnzymechemistryRNA HelicasesJournal of Viral Hepatitis
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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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Structures of Alkaloid Biosynthetic Glucosidases Decode Substrate Specificity

2011

Two similar enzymes with different biosynthetic function in one species have evolved to catalyze two distinct reactions. X-ray structures of both enzymes help reveal their most important differences. The Rauvolfia alkaloid biosynthetic network harbors two O-glucosidases: raucaffricine glucosidase (RG), which hydrolyses raucaffricine to an intermediate downstream in the ajmaline pathway, and strictosidine glucosidase (SG), which operates upstream. RG converts strictosidine, the substrate of SG, but SG does not accept raucaffricine. Now elucidation of crystal structures of RG, inactive RG-E186Q mutant, and its complexes with ligands dihydro-raucaffricine and secologanin reveals that it is the…

Models MolecularRauvolfiaStereochemistryIridoid GlucosidesMolecular Sequence DataMutantCrystallography X-RayBiochemistryRauwolfiaSubstrate SpecificityEvolution Molecularchemistry.chemical_compoundHydrolaseSerineAmino Acid SequenceVinca AlkaloidsPlant Proteinschemistry.chemical_classificationBinding SitesbiologyTryptophanSubstrate (chemistry)General Medicinebiology.organism_classificationKineticsEnzymechemistryBiochemistryStrictosidinebiology.proteinMolecular MedicineSecologaninGlucosidasesGlucosidasesProtein BindingACS Chemical Biology
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