Search results for "Src homology domain"

showing 10 items of 10 documents

Structure of SNX9 SH3 in complex with a viral ligand reveals the molecular basis of its unique specificity for alanine-containing class I SH3 motifs

2021

Class I SH3 domain-binding motifs generally comply with the consensus sequence [R/K]x0PxxP, the hydrophobic residue 0 being proline or leucine. We have studied the unusual 0 = Ala-specificity of SNX9 SH3 by determining its complex structure with a peptide present in eastern equine encephalitis virus (EEEV) nsP3. The structure revealed the length and composition of the n-Src loop as important factors determining specificity. We also compared the affinities of EEEV nsP3 peptide, its mutants, and cellular ligands to SNX9 SH3. These data suggest that nsP3 has evolved to minimize reduction of conformational entropy upon binding, hence acquiring stronger affinity, enabling takeover of SNX9. The R…

DYNAMICSPROLINE-RICH PEPTIDESviruksetPROTEINSvirusesHTLV-1 GagLigandsEVOLUTIONARY CONSERVATIONalfaviruksetsrc Homology DomainsHIGH-AFFINITYretroviruksetDOMAINStructural BiologyBINDINGAnimalsHorsesMolecular Biologysoluviestintä11832 Microbiology and virologyAlanineBinding SitesPXXP MOTIFSisothermal titration calorimetrySH3solution NMR spectroscopyEEEV nsP3HIV-11182 Biochemistry cell and molecular biologyproteiinitCHEMICAL-SHIFTS3111 BiomedicinePeptidesSNX9Protein Binding
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Genome-Wide Inhibition of Pro-atherogenic Gene Expression by Multi-STAT Targeting Compounds as a Novel Treatment Strategy of CVDs.

2018

Cardiovascular diseases (CVDs), including atherosclerosis, are globally the leading cause of death. Key factors contributing to onset and progression of atherosclerosis include the pro-inflammatory cytokines Interferon (IFN)a and IFN? and the Pattern Recognition Receptor (PRR) Toll-like receptor 4 (TLR4). Together, they trigger activation of Signal Transducer and Activator of Transcription (STAT)s. Searches for compounds targeting the pTyr-SH2 interaction area of STAT3, yielded many small molecules, including STATTIC and STX-0119. However, many of these inhibitors do not seem STAT3-specific. We hypothesized that multi-STAT-inhibitors that simultaneously block STAT1, STAT2, and STAT3 activit…

lcsh:Immunologic diseases. Allergy0301 basic medicineMaleIn silicoImmunologyGene ExpressionBiologystatIn silico dockingCell LineSmall Molecule Librariessrc Homology Domains03 medical and health sciencesCVDs treatment strategyImmunology and AllergyAnimalsHumansvascular inflammationSTAT1STAT2STAT3Vascular inflammationCells CulturedOriginal ResearchOxadiazolesGene Expression ProfilingSTATPattern recognition receptorin silico dockingFarmaciaAtherosclerosisCyclic S-OxidesMice Inbred C57BLSTAT Transcription Factors030104 developmental biologyCardiovascular DiseasesTLR4biology.proteinSTAT proteinCancer researchQuinolinesmulti-STAT inhibitorsMulti-STAT inhibitorslcsh:RC581-607Genome-Wide Association StudySignal TransductionFrontiers in immunology
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Deciphering of ADP-induced, phosphotyrosine-dependent signaling networks in human platelets by Src-homology 2 region (SH2)-profiling.

2012

Tyrosine phosphorylation plays a central role in signal transduction controlling many important biological processes. In platelets, the activity of several signaling proteins is controlled by tyrosine phosphorylation ensuring proper platelet activation and aggregation essential for regulation of the delicate balance between bleeding and hemostasis. Here, we applied Src-homology 2 region (SH2)-profiling for deciphering of the phosphotyrosine state of human platelets activated by adenosine diphosphate (ADP). Applying a panel of 31 SH2-domains, rapid and complex regulation of the phosphotyrosine state of platelets was observed after ADP stimulation. Specific inhibition of platelet P2Y receptor…

Blood PlateletsProtein tyrosine phosphataseSH2 domainBiochemistryReceptor tyrosine kinasePhosphorylation cascadesrc Homology Domainschemistry.chemical_compoundReceptors Purinergic P2Y1Tandem Mass SpectrometryHumansProtease-activated receptorProtein phosphorylationIloprostPhosphorylationPhosphotyrosineMolecular BiologybiologyTyrosine phosphorylationPlatelet ActivationCyclic AMP-Dependent Protein KinasesAdenosine MonophosphateReceptors Purinergic P2Y12Cell biologyAdenosine DiphosphateEnzyme ActivationBiochemistrychemistrybiology.proteinPurinergic P2Y Receptor AntagonistsPhosphorylationProtein Processing Post-TranslationalSignal TransductionProteomics
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Cloning and expression of the putative aggregation factor from the marine sponge Geodia cydonium.

2001

Sponges (phylum Porifera) have extensively been used as a model system to study cell-cell interaction on molecular level. Recently, we identified and cloned the putative aggregation receptor (AR) of the sponge Geodia cydonium, which interacts in a heterophilic way with the aggregation factor (AF) complex. In the present study, antibodies against this complex have been raised that abolish the adhesion function of the enriched sponge AF, the AF-Fraction 6B. Using this antibody as a tool, a complete 1.7 kb long cDNA, GEOCYAF, could be isolated from a cDNA library that encodes the putative AF. Its deduced aa sequence in the N-terminal section comprises high similarity to amphiphysin/BIN1 sequen…

DNA ComplementaryBlotting WesternMolecular Sequence DataBiologyModels BiologicalSH3 domainAntibodieslaw.inventionEvolution Molecularsrc Homology DomainslawComplementary DNACell AdhesionEscherichia coliAnimalsAmino Acid SequenceBinding siteCloning MolecularPhylogenyGalectinCell AggregationGene LibraryCloningDose-Response Relationship DrugSequence Homology Amino AcidcDNA libraryCell MembraneCell BiologySequence Analysis DNAMolecular biologyRecombinant ProteinsPoriferaProtein Structure TertiaryAmphiphysinRecombinant DNAPeptidesCell Adhesion MoleculesProtein BindingJournal of cell science
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Evolutionary plasticity of SH3 domain binding by Nef proteins of the HIV-1/SIVcpz lentiviral lineage

2021

The accessory protein Nef of human and simian immunodeficiency viruses (HIV and SIV) is an important pathogenicity factor known to interact with cellular protein kinases and other signaling proteins. A canonical SH3 domain binding motif in Nef is required for most of these interactions. For example, HIV-1 Nef activates the tyrosine kinase Hck by tightly binding to its SH3 domain. An archetypal contact between a negatively charged SH3 residue and a highly conserved arginine in Nef (Arg77) plays a key role here. Combining structural analyses with functional assays, we here show that Nef proteins have also developed a distinct structural strategy—termed the "R-clamp”—that favors the formation …

RNA virusesviruksetvirusesSimian Acquired Immunodeficiency SyndromeHIV InfectionsPathology and Laboratory MedicineSH3 domainWhite Blood CellsImmunodeficiency VirusesAnimal CellsMedicine and Health SciencesBiology (General)MammalsGenetics11832 Microbiology and virology0303 health sciencesKinase030302 biochemistry & molecular biologyEukaryotavirus diseasesTransfection3. Good healthSIVMedical MicrobiologyViral PathogensViral evolutionVirusesVertebratesProto-Oncogene Proteins c-hckApesSimian Immunodeficiency VirusPathogensCellular TypesTyrosine kinaseResearch ArticlePrimateskinaasitEvolutionary ImmunologyLineage (genetic)QH301-705.5Immune CellsImmunologyevoluutioBiologyTransfectionResearch and Analysis MethodsHIV-tartuntaMicrobiologyViral EvolutionEvolution Molecularsrc Homology Domains03 medical and health sciencesVirologyRetrovirusesGeneticsAnimalsHumansLuciferaseAmino Acid Sequencenef Gene Products Human Immunodeficiency VirusChimpanzeesMolecular Biology TechniquesMicrobial PathogensMolecular Biology030304 developmental biologyEvolutionary BiologyBlood CellsSequence Homology Amino AcidMacrophagesLentivirusOrganismsBiology and Life SciencesHIVCell BiologyRC581-607Organismal Evolution3121 General medicine internal medicine and other clinical medicineMicrobial EvolutionAmniotesHIV-1ParasitologySalt bridgeproteiinitImmunologic diseases. AllergyZoology
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Selective Inhibition of STAT3 with Respect to STAT1: Insights from Molecular Dynamics and Ensemble Docking Simulations

2016

STAT3 protein, which is known to be involved in cancer development, is a promising target for anticancer therapy. Successful inhibitors of STAT3 should not affect an activity of closely related protein STAT1, which makes their development challenging. The mechanisms of selectivity of several existing STAT3 inhibitors are not clear. In this work, we studied molecular mechanisms of selectivity of 13 experimentally tested STAT3 inhibitors by means of extensive molecular dynamics and ensemble docking simulations. It is shown that all studied inhibitors bind to the large part of the protein surface in an unspecific statistical manner. The binding to the dimerization interface of the SH2 domain, …

STAT3 Transcription Factor0301 basic medicine[ SDV.BBM.BP ] Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsStereochemistryGeneral Chemical Engineering[SDV.CAN]Life Sciences [q-bio]/CancerMolecular Dynamics SimulationLibrary and Information SciencesBiologySelective inhibitionSH2 domain01 natural sciencesMolecular Docking SimulationSubstrate Specificity[ SDV.CAN ] Life Sciences [q-bio]/Cancersrc Homology Domains03 medical and health sciencesMolecular dynamics[SDV.SP.MED]Life Sciences [q-bio]/Pharmaceutical sciences/Medication[CHIM]Chemical SciencesSTAT1STAT3ComputingMilieux_MISCELLANEOUS010405 organic chemistry[ SDV.SP.MED ] Life Sciences [q-bio]/Pharmaceutical sciences/MedicationGeneral Chemistry0104 chemical sciences3. Good healthComputer Science ApplicationsMolecular Docking Simulation[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsSTAT1 Transcription Factor030104 developmental biologyDocking (molecular)Biophysicsbiology.proteinSelectivity
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Src proteins/src genes: from sponges to mammals

2004

The genome of marine sponge Suberites domuncula, a member of the most ancient and most simple metazoan phylum Porifera, encodes at least five genes for Src-type proteins, more than, i.e., Caenorhabditis elegans or Drosophila melanogaster (two in each). Three proteins, SRC1SD, SRC2SD and SRC3SD, were fully characterized. The overall homology (identity+similarity) among the three S. domuncula Srcs (68-71%) is much lower than the sequence conservation between orthologous Src proteins from freshwater sponges (82-85%). It is therefore very likely that several src genes/proteins were already present in the genome of Urmetazoa, the hypothetical metazoan ancestor. We have identified in the S. domun…

DNA Complementaryanimal structuresMolecular Sequence DataProto-Oncogene Proteins pp60(c-src)SH2 domainHomology (biology)SH3 domainEvolution Molecularsrc Homology DomainsExonGeneticsAnimalsProtein IsoformsAmino Acid SequenceCloning MolecularGenePhylogenyMammalsGeneticsSequence Homology Amino AcidbiologyIntronDNASequence Analysis DNAGeneral Medicinebiology.organism_classificationIntronsPoriferaSuberites domunculaSequence AlignmentProto-oncogene tyrosine-protein kinase SrcGene
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Mona/Gads SH3C binding to hematopoietic progenitor kinase 1 (HPK1) combines an atypical SH3 binding motif, R/KXXK, with a classical PXXP motif embedd…

2004

Hematopoietic progenitor kinase 1 (HPK1) is implicated in signaling downstream of the T cell receptor. Its non-catalytic, C-terminal half contains several prolinerich motifs, which have been shown to interact with different SH3 domain-containing adaptor proteins in vitro. One of these, Mona/Gads, was also shown to bind HPK1 in mouse T cells in vivo. The region of HPK1 that binds to the Mona/Gads C-terminal SH3 domain has been mapped and shows only very limited similarity to a recently identified high affinity binding motif in SLP-76, another T-cell adaptor. Using isothermal titration calorimetry and x-ray crystallography, the binding of the HPK1 motif to Mona/Gads SH3C has now been characte…

Models MolecularTime FactorsProtein ConformationAmino Acid MotifsMolecular Sequence DataPlasma protein bindingBiologyCalorimetryProtein Serine-Threonine KinasesCrystallography X-RayBiochemistrySH3 domainProtein Structure Secondarysrc Homology DomainsMiceProtein structureAnimalsHumansAmino Acid SequenceMolecular BiologyPeptide sequencePolyproline helixAdaptor Proteins Signal TransducingSequence Homology Amino AcidSignal transducing adaptor proteinIsothermal titration calorimetryCell BiologyPhosphoproteinsCell biologyProtein Structure TertiaryCrystallographyKineticsPXXP MotifCarrier ProteinsPeptidesProtein BindingThe Journal of biological chemistry
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Structural Basis of the High Affinity Interaction between the Alphavirus Nonstructural Protein-3 (nsP3) and the SH3 Domain of Amphiphysin-2

2016

We show that a peptide from Chikungunya virus nsP3 protein spanning residues 1728–1744 binds the amphiphysin-2 (BIN1) Src homology-3 (SH3) domain with an unusually high affinity (Kd 24 nM). Our NMR solution complex structure together with isothermal titration calorimetry data on several related viral and cellular peptide ligands reveal that this exceptional affinity originates from interactions between multiple basic residues in the target peptide and the extensive negatively charged binding surface of amphiphysin-2 SH3. Remarkably, these arginines show no fixed conformation in the complex structure, indicating that a transient or fluctuating polyelectrostatic interaction accounts for this …

0301 basic medicinenuclear magnetic resonance (NMR)Amino Acid MotifsStatic ElectricityPeptideTarget peptidePlasma protein bindingViral Nonstructural ProteinsBiologyhost-pathogen interactionBiochemistrySH3 domainsrc Homology Domainsamphiphysin SH3Structure-Activity Relationship03 medical and health sciencesProtein structuredynaminHumansShort linear motifprotein structureNuclear Magnetic Resonance BiomolecularMolecular BiologySrc homology 3 domain (SH3 domain)Adaptor Proteins Signal Transducingchemistry.chemical_classificationTumor Suppressor Proteinsta1182Nuclear ProteinsIsothermal titration calorimetryCell Biologyintrinsically disordered protein030104 developmental biologychemistryBiochemistrynsP3Protein Structure and FoldingAmphiphysinBiophysicsPeptidesChikungunya virusProtein BindingJournal of Biological Chemistry
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The yopJ locus is required for Yersinia-mediated inhibition of NF-kappaB activation and cytokine expression: YopJ contains a eukaryotic SH2-like doma…

1998

Upon exposure to bacteria, eukaryotic cells activate signalling pathways that result in the increased expression of several defence-related genes. Here, we report that the yopJ locus of the enteropathogen Yersinia pseudotuberculosis encodes a protein that inhibits the activation of NF-kappaB transcription factors by a mechanism(s), which prevents the phosphorylation and subsequent degradation of the inhibitor protein IkappaB. Consequently, eukaryotic cells infected with YopJ-expressing Yersinia become impaired in NF-kappaB-dependent cytokine expression. In addition, the blockage of inducible cytokine production coincides with yopJ-dependent induction of apoptosis. Interestingly, the YopJ pr…

Transcriptional Activationmedicine.medical_treatmentMolecular Sequence DataApoptosisBiologySH2 domainTransfectionMicrobiologysrc Homology DomainsGenes ReportermedicineYersinia pseudotuberculosisHumansAmino Acid SequenceMolecular BiologyGeneTranscription factorCells CulturedSrc homology domainVirulenceTumor Necrosis Factor-alphaMacrophagesNF-kappa BYersiniosisGene Expression Regulation Bacterialbiology.organism_classificationmedicine.diseaseFlow CytometryMolecular biologyCell biologyCytokineYersinia pseudotuberculosisPhosphorylationCytokinesBacterial Outer Membrane ProteinsHeLa CellsPlasmidsMolecular microbiology
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