Search results for "DOMAINS"

showing 10 items of 269 documents

Activation of the p75 neurotrophin receptor through conformational rearrangement of disulphide-linked receptor dimers.

2009

Ligand-mediated dimerization has emerged as a universal mechanism of growth factor receptor activation. Recent structural studies have shown that neurotrophins interact with dimers of the p75 neurotrophin receptor (p75NTR), but the actual mechanism of receptor activation has remained elusive. Here we show that p75NTR forms disulphide-linked dimers independently of neurotrophin binding through the highly conserved Cys257 in its transmembrane domain. Mutation of Cys257 abolished neurotrophin-dependent receptor activity but did not affect downstream signaling by the p75NTR/NgR/Lingo-1 complex in response to MAG, indicating the existence of distinct, ligand-specific activation mechanisms for p7…

Protein ConformationMutantNeuronesReceptor Nerve Growth FactorMiceProtein structureChlorocebus aethiopsNerve Growth FactorLow-affinity nerve growth factor receptorRNA Small InterferingReceptorskin and connective tissue diseasesReceptors neuralsCells CulturedNeuronsCell DeathGeneral NeuroscienceNF-kappa BCell biologyTransmembrane domainSIGNALINGOligopeptidesNeurotrophinProtein BindingSignal Transductionmusculoskeletal diseasesPROTEINSNeuroscience(all)Green Fluorescent ProteinsNerve Tissue ProteinsReceptors Nerve Growth FactorSuperior Cervical GanglionBiologyTransfectionMOLNEUROArticleGrowth factor receptorAnimalsHumansProtein Interaction Domains and MotifsReceptors Growth FactorCysteineBinding SitesMembrane Proteinsbiological factorsRatsnervous systemAnimals NewbornNeurotrophin bindingMutationbiology.proteinsense organsProtein MultimerizationrhoA GTP-Binding ProteinProteïnesNeuron
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Conformational clamping by a membrane ligand activates the EphA2 receptor

2021

AbstractThe EphA2 receptor is a promising drug target for cancer treatment, since EphA2 activation can inhibit metastasis and tumor progression. It has been recently described that the TYPE7 peptide activates EphA2 using a novel mechanism that involves binding to the single transmembrane domain of the receptor. TYPE7 is a conditional transmembrane (TM) ligand, which only inserts into membranes at neutral pH in the presence of the TM region of EphA2. However, how membrane interactions can activate EphA2 is not known. We systematically altered the sequence of TYPE7 to identify the binding motif used to activate EphA2. With the resulting six peptides, we performed biophysical and cell migratio…

Protein ConformationSequence HomologyTm ligandsPeptideMolecular Dynamics SimulationLigandsReceptor tyrosine kinaseArticleBimolecular fluorescence complementationProtein DomainsStructural BiologyCell MovementCell surface receptorTumor Cells CulturedHumansAmino Acid SequenceReceptorMolecular BiologyMelanomachemistry.chemical_classificationBinding SitesMembranesbiologyChemistryReceptor EphA2Membrane ProteinsLigand (biochemistry)Peptide FragmentsTransmembrane proteinTransmembrane domainMembranebiology.proteinBiophysicsProtein MultimerizationProtein Binding
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Methodological approaches for the analysis of transmembrane domain interactions: A systematic review

2021

The study of protein-protein interactions (PPI) has proven fundamental for the understanding of the most relevant cell processes. Any protein domain can participate in PPI, including transmembrane (TM) segments that can establish interactions with other TM domains (TMDs). However, the hydrophobic nature of TMDs and the environment they occupy complicates the study of intramembrane PPI, which demands the use of specific approaches and techniques. In this review, we will explore some of the strategies available to study intramembrane PPI in vitro, in vivo, and, in silico, focusing on those techniques that could be carried out in a standard molecular biology laboratory regarding its previous e…

Protein FoldingBacteriaChemistryIn silicoProtein domainBiophysicsMembrane ProteinsCell CommunicationCell BiologyComputational biologyBiochemistryTransmembrane proteinIn vitroProtein–protein interactionTransmembrane domainProtein DomainsMembrane proteinProtein foldingProtein Interaction MapsHydrophobic and Hydrophilic InteractionsBiochimica et Biophysica Acta (BBA) - Biomembranes
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Targeting SARS-CoV-2 RBD Interface: a Supervised Computational Data-Driven Approach to Identify Potential Modulators

2020

Coronavirus disease 2019 (COVID-19) has spread out as a pandemic threat affecting over 2 million people. The infectious process initiates via binding of SARS-CoV-2 Spike (S) glycoprotein to host angiotensin-converting enzyme 2 (ACE2). The interaction is mediated by the receptor-binding domain (RBD) of S glycoprotein, promoting host receptor recognition and binding to ACE2 peptidase domain (PD), thus representing a promising target for therapeutic intervention. Herein, we present a computational study aimed at identifying small molecules potentially able to target RBD. Although targeting PPI remains a challenge in drug discovery, our investigation highlights that interaction between SARS-CoV…

Protein domainPneumonia ViralDruggabilityDrug Evaluation Preclinicalprotein-protein interactionsComputational biologyBiologyMolecular Dynamics SimulationPeptidyl-Dipeptidase AMolecular dynamics01 natural sciencesBiochemistryMolecular Docking SimulationAntiviral Agentsdockingmolecular dynamicProtein–protein interactionSmall Molecule LibrariesBetacoronavirusProtein DomainsDrug DiscoveryHumansGeneral Pharmacology Toxicology and PharmaceuticsPandemicsPharmacologyFull Paperpharmacophore010405 organic chemistryDrug discoverySARS-CoV-2Organic ChemistryCOVID-19Small molecule0104 chemical sciencesProtein-Protein InteractionMolecular Docking Simulation010404 medicinal & biomolecular chemistryDocking (molecular)Spike Glycoprotein CoronavirusdockingMolecular MedicineAngiotensin-Converting Enzyme 2PharmacophoreCoronavirus InfectionsProtein Binding
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The cytosolic Arabidopsis thaliana cysteine desulfurase ABA3 delivers sulfur to the sulfurtransferase STR18

2020

ABSTRACTThe biosynthesis of many sulfur-containing molecules depends on cysteine as a sulfur source. Cysteine desulfurase (CD) and rhodanese (Rhd) domain-containing protein families participate in the trafficking of sulfur for various metabolic pathways in bacteria and human, but their connection is not yet described in plants. The existence of natural chimeric proteins, however, containing both CD and Rhd domains in specific bacterial genera suggests a general interaction between both proteins. We report here the biochemical relationships between two cytosolic proteins from Arabidopsis thaliana, a Rhd domain containing protein, the sulfurtransferase 18 (STR18), and a CD isoform referred to…

Protein familyArabidopsisSulfurtransferaseRhodaneseBiochemistry03 medical and health scienceschemistry.chemical_compoundCytosolProtein DomainsArabidopsis thalianaCysteineMolecular Biology030304 developmental biology0303 health sciencesbiologyArabidopsis ProteinsCysteine desulfurase030302 biochemistry & molecular biologyCell Biologybiology.organism_classificationFusion proteinThiosulfate SulfurtransferaseCarbon-Sulfur LyasesBiochemistrychemistrySulfurtransferasesMolybdenum cofactorSulfurCysteine
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Effects of sulindac sulfide on the membrane architecture and the activity of gamma-secretase.

2007

gamma-Secretase is a membrane-embedded multi-protein complex that catalyzes the final cut of the Alzheimer's disease-related amyloid precursor protein (APP) to amyloid-beta peptides of variable length (37-43 amino acids) via an unusual intramembrane cleavage. Recent findings propose that some commonly used non-steroidal anti-inflammatory drugs (NSAIDs) have the ability to modulate specifically gamma-secretase activity without inhibiting the enzyme as a whole. These drugs may shift the processing of APP from the longer amyloid-beta 42 peptide towards shorter, less fibrillogenic and less toxic amyloid-beta species. We hypothesize that gamma-secretase activity, as an enzyme that is strictly as…

Protein subunitBlotting WesternPeptideCHO CellsSarcoplasmic Reticulum Calcium-Transporting ATPasesCellular and Molecular NeuroscienceAmyloid beta-Protein PrecursorCricetulusMembrane MicrodomainsSulindacCricetinaemental disordersAmyloid precursor proteinPresenilin-1AnimalsHumansLipid raftCells CulturedPharmacologychemistry.chemical_classificationbiologyAnti-Inflammatory Agents Non-SteroidalCell MembraneP3 peptideAmino acidMembraneBiochemistrychemistrybiology.proteinBiophysicsAmyloid Precursor Protein SecretasesAmyloid precursor protein secretaseNeuropharmacology
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Perturbed interactions of mutant proteolipid protein/DM20 with cholesterol and lipid rafts in oligodendroglia: implications for dysmyelination in spa…

2006

Missense mutations in the humanPLP1gene lead to dysmyelinating diseases with a broad range of clinical severity, ranging from severe Pelizaeus–Merzbacher disease (PMD) to milder spastic paraplegia type 2 (SPG-2). The molecular pathology has been generally attributed to endoplasmic reticulum (ER) retention of misfolded proteolipid protein (PLP) (and its splice isoform DM20) and induction of the unfolded protein response. As opposed to previous studies of heterologous expression systems, we have analyzed PLP/DM20 trafficking in oligodendroglial cells, thereby revealing differences between PMD and SPG-2-associated PLP/DM20 isoforms. PLPA242Vand DM20A242V(jimpy-msdin mice), associated with seve…

Proteolipid protein 1Time FactorsLeupeptinsBlotting WesternGene Expressionchemical and pharmacologic phenomenaNerve Tissue ProteinsBiologyProtein degradationCysteine Proteinase InhibitorsTransfectionMiceMice Neurologic MutantsCricetulusMembrane MicrodomainsMutant proteinimmune system diseasesCricetinaeAnimalsImmunoprecipitationMyelin Proteolipid ProteinLipid raftCells CulturedGeneral NeuroscienceEndoplasmic reticulumCholesterol bindingER retentionArticlesImmunohistochemistryCell biologynervous system diseasesOligodendrogliaProtein TransportCholesterolBiochemistryUnfolded protein responselipids (amino acids peptides and proteins)Mutant ProteinsSubcellular FractionsThe Journal of neuroscience : the official journal of the Society for Neuroscience
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Assessing the low complexity of protein sequences via the low complexity triangle.

2020

Background Proteins with low complexity regions (LCRs) have atypical sequence and structural features. Their amino acid composition varies from the expected, determined proteome-wise, and they do not follow the rules of structural folding that prevail in globular regions. One way to characterize these regions is by assessing the repeatability of a sequence, that is, calculating the local propensity of a region to be part of a repeat. Results We combine two local measures of low complexity, repeatability (using the RES algorithm) and fraction of the most frequent amino acid, to evaluate different proteomes, datasets of protein regions with specific features, and individual cases of proteins…

ProteomeProteomesComputer scienceProtein SequencingBiochemistryDatabase and Informatics MethodsSequence Analysis ProteinProtein methodsPeptide sequencechemistry.chemical_classification0303 health sciencesSequenceMultidisciplinary030302 biochemistry & molecular biologyQRGenomicsAmino acidTandem RepeatsProteomeAmino Acid AnalysisMedicineSequence AnalysisResearch ArticleRepetitive Sequences Amino AcidBioinformaticsSequence analysisScienceResearch and Analysis MethodsGenome Complexity03 medical and health sciencesProtein DomainsAmino Acid Sequence AnalysisTandem repeatGeneticsHumansFraction (mathematics)Repeated SequencesAmino Acid SequenceMolecular Biology TechniquesSequencing TechniquesRepresentation (mathematics)Molecular Biology030304 developmental biologyMolecular Biology Assays and Analysis Techniquesbusiness.industryBiology and Life SciencesProteinsComputational BiologyPattern recognitionchemistryGlobular ProteinsArtificial intelligencebusinessPLoS ONE
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Proteome-wide comparison between the amino acid composition of domains and linkers

2018

Objective Amino acid composition is a sequence feature that has been extensively used to characterize proteomes of many species and protein families. Yet the analysis of amino acid composition of protein domains and the linkers connecting them has received less attention. Here, we perform both a comprehensive full-proteome amino acid composition analysis and a similar analysis focusing on domains and linkers, to uncover domain- or linker-specific differential amino acid usage patterns. Results The amino acid composition in the 38 proteomes studied showcase the greater variability found in archaea and bacteria species compared to eukaryotes. When focusing on domains and linkers, we describe …

Proteomics570BacteriaProteomeAmino acid compositionlcsh:Rlcsh:MedicineEukaryotaArchaea570 Life sciencesResearch Notelcsh:Biology (General)Sequence Analysis ProteinCatalytic DomainDomainsAmino Acid SequenceLinkerslcsh:Science (General)lcsh:QH301-705.5570 Biowissenschaftenlcsh:Q1-390BMC Research Notes
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Membrane vesicles containing matrix metalloproteinase-9 and fibroblast growth factor-2 are released into the extracellular space from mouse mesoangio…

2010

Certain proteins, including fibroblast growth factor-2 (FGF-2) and matrix metalloproteinase-9 (MMP-9), have proved very effective in increasing the efficacy of mesoangioblast stem cell therapy in repairing damaged tissue. We provide the first evidence that mouse mesoangioblast stem cells release FGF-2 and MMP-9 in their active form through the production of membrane vesicles. These vesicles are produced and turned over continuously, but are stable for some time in the extracellular milieu. Mesoangioblasts shed membrane vesicles even under oxygen tensions that are lower than those typically used for cell culture and more like those of mouse tissues. These findings suggest that mesoangioblast…

ProteomicsTime FactorsPhysiologyClinical BiochemistryBiologyFibroblast growth factorCell LineMiceMembrane MicrodomainsTubulinParacrine CommunicationmedicineExtracellularAnimalsSecretionSettore BIO/06 - Anatomia Comparata E CitologiaFibroblastCytoskeletonMembrane vesicles MMP9 FGF2 mouse mesoangioblastMesoangioblastSecretory VesiclesVesicleBiological TransportMesenchymal Stem CellsCell BiologyCell biologyOxygenmedicine.anatomical_structureMatrix Metalloproteinase 9Cell cultureFibroblast Growth Factor 2Stem cellExtracellular Space
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