Search results for "Interaction domains"

showing 10 items of 46 documents

Determination of enrichment factors for modified RNA in MeRIP experiments

2019

In the growing field of RNA modification, precipitation techniques using antibodies play an important role. However, little is known about their specificities and protocols are missing to assess their effectiveness. Here we present a method to assess enrichment factors after MeRIP-type pulldown experiments, here exemplified with a commercial antibody against N6-methyladenosine (m6A). Testing different pulldown and elution conditions, we measure enrichment factors of 4-5 using m6A-containing mRNAs against an unmodified control of identical sequence. Both types of mRNA carry 32P labels at different nucleotides, allowing their relative quantification in a mixture after digestion to nucleotides…

Models MolecularAdenosineAbsolute quantificationMethylationProtein Structure SecondaryGeneral Biochemistry Genetics and Molecular BiologyViral Proteins03 medical and health sciencesAdenosine TriphosphateRNA modificationEscherichia coliHumansImmunoprecipitationProtein Interaction Domains and MotifsNucleotideRNA MessengerMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesMessenger RNACell-Free SystemChemistryElution030302 biochemistry & molecular biologyRNADNA-Directed RNA PolymerasesBiochemistryImmunoglobulin GIsotope LabelingChromatography Thin LayerPhosphorus RadioisotopesProtein BindingMethods
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Synthesis and Inhibitory Studies of Phosphonic Acid Analogues of Homophenylalanine and Phenylalanine towards Alanyl Aminopeptidases.

2020

A library of novel phosphonic acid analogues of homophenylalanine and phenylalanine, containing fluorine and bromine atoms in the phenyl ring, have been synthesized. Their inhibitory properties against two important alanine aminopeptidases, of human (hAPN, CD13) and porcine (pAPN) origin, were evaluated. Enzymatic studies and comparison with literature data indicated the higher inhibitory potential of the homophenylalanine over phenylalanine derivatives towards both enzymes. Their inhibition constants were in the submicromolar range for hAPN and the micromolar range for pAPN, with 1-amino-3-(3-fluorophenyl) propylphosphonic acid (compound 15c) being one of the best low-molecular inhibitors …

Models MolecularProtein Conformation alpha-HelicalMolecular modelStereochemistryPhosphorous AcidsSwinePhenylalaninelcsh:QR1-502PhenylalanineCD13 Antigenscomputer-aided simulationsInhibitory postsynaptic potential01 natural sciencesBiochemistrylcsh:MicrobiologyArticlePhenylalanine derivativesSubstrate SpecificitySmall Molecule Libraries03 medical and health sciencesStructure-Activity RelationshipAnimalsHumansProtein Interaction Domains and MotifsEnzyme Inhibitorsphosphonic acid inhibitorsMolecular Biology030304 developmental biologyAlaninechemistry.chemical_classification0303 health sciencesInhibitory potentialBinding Sites010405 organic chemistryChemistryAminobutyratesFluorineBromine0104 chemical sciencesIsoenzymesKineticsEnzymehuman and porcine alanine aminopeptidasefluorine and bromine substitutionThermodynamicsProtein Conformation beta-StrandProtein BindingBiomolecules
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The Protein Structure Context of PolyQ Regions.

2016

Proteins containing glutamine repeats (polyQ) are known to be structurally unstable. Abnormal expansion of polyQ in some proteins exceeding a certain threshold leads to neurodegenerative disease, a symptom of which are protein aggregates. This has led to extensive research of the structure of polyQ stretches. However, the accumulation of contradictory results suggests that protein context might be of importance. Here we aimed to evaluate the structural context of polyQ regions in proteins by analysing the secondary structure of polyQ proteins and their homologs. The results revealed that the secondary structure in polyQ vicinity is predominantly random coil or helix. Importantly, the region…

Models MolecularProtein Conformation alpha-HelicalProtein Structure ComparisonProtein StructureSaccharomyces cerevisiae ProteinsGlutaminelcsh:MedicineNerve Tissue ProteinsSaccharomyces cerevisiaePlant ScienceResearch and Analysis MethodsBiochemistryPlant Roots570 Life sciencesDatabase and Informatics MethodsProtein Structure DatabasesMacromolecular Structure AnalysisHumansProtein Interaction Domains and MotifsAmino AcidsDatabases ProteinProtein Interactionslcsh:ScienceMolecular BiologyMediator ComplexOrganic CompoundsPlant AnatomyAcidic Amino AcidsOrganic Chemistrylcsh:RChemical CompoundsBiology and Life SciencesProteinsRoot StructureChemistryBiological DatabasesProtein-Protein InteractionsPhysical Scienceslcsh:QStructural ProteinsProtein Structure DeterminationPeptidesResearch Article570 BiowissenschaftenPLoS ONE
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Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family.

2020

Lyme disease is the most widespread vector‐transmitted disease in North America and Europe, caused by infection with Borrelia burgdorferi sensu lato complex spirochetes. We report the solution NMR structure of the B. burgdorferi outer surface lipoprotein BBP28, a member of the multicopy lipoprotein (mlp) family. The structure comprises a tether peptide, five α‐helices and an extended C‐terminal loop. The fold is similar to that of Borrelia tunicate outer surface protein BTA121, which is known to bind lipids. These results contribute to the understanding of Lyme disease pathogenesis by revealing the molecular structure of a protein from the widely found mlp family. This article is protected …

Models MolecularProtein Conformation alpha-HelicalProtein familyLipoproteinsGenetic VectorsGene ExpressionPeptideBiochemistryMicrobiologyPathogenesis03 medical and health sciencesLyme diseaseStructural BiologyBorreliamedicineEscherichia coliHumansProtein Interaction Domains and MotifsAmino Acid SequenceBorrelia burgdorferiCloning MolecularMolecular BiologyNuclear Magnetic Resonance Biomolecular030304 developmental biologychemistry.chemical_classification0303 health sciencesLyme DiseasebiologySequence Homology Amino AcidBorrelia030302 biochemistry & molecular biologybacterial infections and mycosesbiology.organism_classificationmedicine.diseaseRecombinant ProteinsProtein Structure TertiaryOuter surface proteinchemistryBorrelia burgdorferiProtein Conformation beta-StrandSequence AlignmentLipoproteinBacterial Outer Membrane ProteinsProteinsREFERENCES
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Mass Spectrometry and Structural Biology Techniques in the Studies on the Coronavirus-Receptor Interaction

2020

Mass spectrometry and some other biophysical methods, have made substantial contributions to the studies on severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and human proteins interactions. The most interesting feature of SARS-CoV-2 seems to be the structure of its spike (S) protein and its interaction with the human cell receptor. Mass spectrometry of spike S protein revealed how the glycoforms are distributed across the S protein surface. X-ray crystallography and cryo-electron microscopy made huge impact on the studies on the S protein and ACE2 receptor protein interaction, by elucidating the three-dimensional structures of these proteins and their conformational changes. The…

Models MolecularProtein Conformation alpha-HelicalvirusesGene ExpressionPharmaceutical ScienceReviewPlasma protein bindingSevere Acute Respiratory Syndromemedicine.disease_causeAnalytical Chemistry0302 clinical medicineDrug Discovery030212 general & internal medicineReceptorPeptide sequenceCoronavirus0303 health sciencesChemistrySevere acute respiratory syndrome-related coronavirusBiochemistryChemistry (miscellaneous)Host-Pathogen InteractionsSpike Glycoprotein CoronavirusReceptors VirusMolecular MedicineAngiotensin-Converting Enzyme 2Coronavirus InfectionsProtein BindingglycosylationSARS coronavirusPneumonia Viralstructural techniquesSequence alignmentPeptidyl-Dipeptidase AMass spectrometrylcsh:QD241-441Betacoronavirus03 medical and health scienceslcsh:Organic chemistryspike protein-ACE2 interactionmedicineHumansProtein Interaction Domains and MotifsAmino Acid SequencePhysical and Theoretical ChemistryBinding sitePandemics030304 developmental biologyBinding SitesSARS-CoV-2Organic ChemistryCOVID-19MSStructural biologyProtein Conformation beta-StrandSequence AlignmentMolecules
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Trimeric HIV Env provides epitope occlusion mediated by hypervariable loops

2014

AbstractHypervariable loops of HIV-1 Env protein gp120 are speculated to play roles in the conformational transition of Env to the receptor binding-induced metastable state. Structural analysis of full-length Env-based immunogens, containing the entire V2 loop, displayed tighter association between gp120 subunits, resulting in a smaller trimeric diameter than constructs lacking V2. A prominent basal quaternary location of V2 and V3′ that challenges previous reports would facilitate gp41-independent gp120-gp120 interactions and suggests a quaternary mechanism of epitope occlusion facilitated by hypervariable loops. Deletion of V2 resulted in dramatic exposure of basal, membrane-proximal gp41…

Models MolecularProtein ConformationvirusesHuman immunodeficiency virus (HIV)[CHIM.THER]Chemical Sciences/Medicinal ChemistryPlasma protein bindingHIV Envelope Protein gp120medicine.disease_causeEnv ProteinEpitopeenv Gene ProductsEpitopesProtein structureModelsComputingMilieux_MISCELLANEOUSSequence DeletionGeneticsMultidisciplinary[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]Transition (genetics)biologyenv Gene Products Human Immunodeficiency Virusvirus diseaseshypervariable loopsHIV Envelope Protein gp41[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]3. Good health[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]CD4 AntigensHIV/AIDSAntibodyHuman Immunodeficiency VirusProtein BindingEnvGp41ArticleVaccine RelatedGenetics[CHIM.CRIS]Chemical Sciences/CristallographymedicineHumansProtein Interaction Domains and Motifs[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]AntigensVaccine Related (AIDS)Preventionta1182Molecular[SDV.IMM.IMM]Life Sciences [q-bio]/Immunology/ImmunotherapyCD4Peptide Fragmentsgp120Good Health and Well BeingHIV-1biology.proteinImmunizationProtein MultimerizationproteinScientific Reports
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A human CCT5 gene mutation causing distal neuropathy impairs hexadecamer assembly in an archaeal model

2014

Chaperonins mediate protein folding in a cavity formed by multisubunit rings. The human CCT has eight non-identical subunits and the His147Arg mutation in one subunit, CCT5, causes neuropathy. Knowledge is scarce on the impact of this and other mutations upon the chaperone's structure and functions. To make progress, experimental models must be developed. We used an archaeal mutant homolog and demonstrated that the His147Arg mutant has impaired oligomeric assembly, ATPase activity, and defective protein homeostasis functions. These results establish for the first time that a human chaperonin gene defect can be reproduced and studied at the molecular level with an archaeal homolog. The major…

Models MolecularProtein FoldingProtein ConformationProtein subunitMutantMolecular Sequence Datahuman CCT5 gene mutation molecular dynamics neuropathy archaeal modelSequence alignmentGene mutationBiologyArticleChaperonin03 medical and health sciences0302 clinical medicineProtein structureHumansProtein Interaction Domains and MotifsAmino Acid Sequence030304 developmental biologyGenetics0303 health sciencesMultidisciplinarySettore BIO/16 - Anatomia UmanaArchaeaSettore CHIM/08 - Chimica FarmaceuticaChaperone (protein)Mutationbiology.proteinThermodynamicsProtein foldingProtein MultimerizationSequence Alignment030217 neurology & neurosurgeryChaperonin Containing TCP-1
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Six amino acids define a minimal dimerization sequence and stabilize a transmembrane helix dimer by close packing and hydrogen bonding

2013

AbstractDistinct amino acid sequences have been described to mediate oligomerization of transmembrane α-helices. However, as the sequence context is crucial to determine specificity in transmembrane helix–helix interaction, the question arises how small a sequence can be without losing specificity. In the present analysis, six amino acids have been identified in the PsbF transmembrane helix dimer, which form the contact region of two interacting helices and are directly involved in helix–helix interactions. However, individual amino acids within the complex sequence pattern only together ensure sequence specificity of the analyzed transmembrane helix–helix interactions by mediating close pa…

Models MolecularStereochemistryDimerRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsCytochrome b559Sequence (biology)Context (language use)Cytochrome b559BiologyBiochemistryProtein Structure Secondarychemistry.chemical_compoundBacterial ProteinsStructural BiologyGeneticsEscherichia coliProtein Interaction Domains and MotifsAmino Acid SequenceDimerization motifMolecular Biologychemistry.chemical_classificationSequence contextHydrogen bondProtein StabilityCell MembraneMembrane ProteinsHelix–helix interactionHydrogen BondingCell BiologyCytochrome b GroupTransmembrane proteinTransmembraneAmino acidTransmembrane domainchemistryDimerizationProtein BindingFEBS Letters
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β2 integrin phosphorylation on Thr758 acts as a molecular switch to regulate 14-3-3 and filamin binding

2008

AbstractLeukocyte integrins of the β2 family are essential for immune cell-cell adhesion. In activated cells, β2 integrins are phosphorylated on the cytoplasmic Thr758, leading to 14-3-3 protein recruitment to the β2 integrin. The mutation of this phosphorylation site impairs cell adhesion, actin reorganization, and cell spreading. Thr758 is contained in a Thr triplet of β2 that also mediates binding to filamin. Here, we investigated the binding of filamin, talin, and 14-3-3 proteins to phosphorylated and unphosphorylated β2 integrins by biochemical methods and x-ray crystallography. 14-3-3 proteins bound only to the phosphorylated integrin cytoplasmic peptide, with a high affinity (Kd, 261…

Models MolecularTalinThreonineanimal structuresFilaminsT-LymphocytesStatic ElectricityImmunologyIntegrinCD18macromolecular substancesPlasma protein bindingIn Vitro TechniquesFilaminBiochemistryJurkat Cells03 medical and health sciencesFilamin bindingContractile Proteins0302 clinical medicineCell AdhesionHumansProtein Interaction Domains and MotifsPhosphorylationCell adhesion030304 developmental biology0303 health sciencesBinding SitesbiologyChemistryMicrofilament ProteinsCell BiologyHematologyIntercellular Adhesion Molecule-1Talin bindingRecombinant ProteinsCell biology14-3-3 ProteinsAmino Acid SubstitutionCD18 AntigensMultiprotein Complexes030220 oncology & carcinogenesisbiology.proteinPhosphorylationProtein BindingBlood
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Structure of the human filamin A actin-binding domain.

2009

Filamin A (FLNa) is a large dimeric protein that binds to actin filaments via its actin-binding domain (ABD). The crystal structure of this domain was solved at 3.2 A resolution. The domain adopts a closed conformation typical of other ABDs, but also forms a dimer both in crystallization conditions and in solution. The structure shows the localization of the residues mutated in patients with periventricular nodular heterotopia or otopalatodigital syndrome. Structural analysis predicts that mutations in both types of disorder may affect actin binding.

Models Molecularanimal structuresDimerFilaminsmacromolecular substancesFilaminCalponin homology domainCrystallography X-Raychemistry.chemical_compoundContractile ProteinsStructural BiologyFLNAHumansProtein Interaction Domains and MotifsActin-binding proteinProtein Structure QuaternaryActinbiologyMicrofilament ProteinsGeneral MedicineActinschemistryStructural Homology ProteinDomain (ring theory)Mutationbiology.proteinBiophysicsBinding domainProtein BindingActa crystallographica. Section D, Biological crystallography
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