Search results for "Protein structure"

showing 10 items of 757 documents

Concerted motions of the integrin-binding loop and the C-terminal tail of the non-RGD disintegrin obtustatin.

2003

Obtustatin is a potent and selective inhibitor of the alpha1beta1 integrin in vitro and of angiogenesis in vivo. It possesses an integrin recognition loop that harbors, in a lateral position, the inhibitory 21KTS23 motif. We report an analysis of the dynamics of the backbone and side-chain atoms of obtustatin by homonuclear NMR methods. Angular mobility has been calculated for 90 assigned cross-peaks from 22 off-resonance rotating frame nuclear Overhauser effect spectroscopy spectra recorded at three magnetic fields. Our results suggest that the integrin binding loop and the C-terminal tail display concerted motions, which can be interpreted by hinge effects. Among the integrin-binding moti…

Models MolecularThreonineIntegrinsMagnetic Resonance SpectroscopyStereochemistryProtein ConformationIntegrinAmino Acid MotifsPlasma protein bindingNuclear Overhauser effectViper VenomsBiochemistryIntegrin alpha1beta1SerineProtein structureDisintegrinSerineThreonineMolecular BiologyIntegrin bindingAlanineModels StatisticalbiologyChemistryHydrogen BondingCell BiologyProtein Structure Tertiarybiology.proteinCollagenPeptidesProtein BindingThe Journal of biological chemistry
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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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New alkaloid antibiotics that target the DNA topoisomerase I of Streptococcus pneumoniae

2011

16 pags, 3 figs, 3 tabs

Models MolecularTopoisomerase-I Inhibitormedicine.disease_causeMicrobiologyBiochemistryCell LineMicrobiology03 medical and health scienceschemistry.chemical_compoundAlkaloidsBacterial ProteinsStreptococcus pneumoniaemedicineHumansAporphineMolecular BiologyEscherichia coli030304 developmental biologychemistry.chemical_classification0303 health sciencesDose-Response Relationship Drugbiology030306 microbiologyTopoisomeraseCell BiologyPhenanthrenesProtein Structure TertiaryAnti-Bacterial Agents3. Good healthStreptococcus pneumoniaeEnzymeDNA Topoisomerases Type IchemistryBiochemistrybiology.proteinDNA supercoilTopoisomerase I InhibitorsGrowth inhibitionJournal of Biological Chemistry 286: 6402-6413 (2011)
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Structural and Functional Basis for Understanding the Biological Significance of P2X7 Receptor

2020

The P2X7 receptor (P2X7R) possesses a unique structure associated to an as yet not fully understood mechanism of action that facilitates cell permeability to large ionic molecules through the receptor itself and/or nearby membrane proteins. High extracellular adenosine triphosphate (ATP) levels—inexistent in physiological conditions—are required for the receptor to be triggered and contribute to its role in cell damage signaling. The inconsistent data on its activation pathways and the few studies performed in natively expressed human P2X7R have led us to review the structure, activation pathways, and specific cellular location of P2X7R in order to analyze its biological relevance. The ATP-…

Models MolecularTranscription GeneticP2X7 receptor physiological rolechannel membrane proteinsAllosteric regulationReviewModels BiologicalCatalysislcsh:ChemistryInorganic ChemistryTransduction (genetics)chemistry.chemical_compoundAdenosine Triphosphateallosteric modulationsmedicineExtracellularAnimalsHumansPhysical and Theoretical ChemistryProtein Structure QuaternaryReceptorlcsh:QH301-705.5Molecular BiologySpectroscopyhuman P2X7 receptor isoformsPolymorphism GeneticCell MembraneOrganic ChemistryGeneral MedicineComputer Science ApplicationsCell biologyATPlcsh:Biology (General)lcsh:QD1-999Mechanism of actionchemistryMembrane proteinP2X7 receptorReceptors Purinergic P2X7medicine.symptomAdenosine triphosphateIntracellularSignal TransductionInternational Journal of Molecular Sciences
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Comparative 11A structure of two molluscan hemocyanins from 3D cryo-electron microscopy

2006

Abstract Hemocyanins are giant extracellular proteins that transport oxygen in the hemolymph of many molluscs. Molluscan hemocyanins are cylindrical decamers or didecamers of a 350–400 kDa subunit that contains seven or eight different covalently linked globular functional units (FUs), arranged in a linear manner. Each FU carries a single copper active site and reversibly binds one dioxygen molecule. As a consequence, the decamer can carry up to 70 or 80 O 2 molecules. Although complete sequence information is now available from several molluscan hemocyanins, many details of the quaternary structure are still unclear, including the topology of the 10 subunits within the decamer. Here we sho…

Models MolecularTransport oxygenCryo-electron microscopyMacromolecular Substancesmedicine.medical_treatmentProtein subunitGeneral Physics and AstronomyHemocyaninStructural BiologyHemolymphmedicineImage Processing Computer-AssistedAnimalsGeneral Materials ScienceProtein Structure QuaternarybiologyResolution (electron density)Cryoelectron MicroscopyActive siteHemocyaninCell BiologyCrystallographyMolluscaHemocyaninsbiology.proteinProtein quaternary structure
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Identification of SNARE complex modulators that inhibit exocytosis from an alpha-helix-constrained combinatorial library.

2003

Synthetic peptides patterned after the proteins involved in vesicle fusion [the so-called SNARE (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor) proteins] are potent inhibitors of SNARE complex assembly and neuronal exocytosis. It is noteworthy that the identification of peptide sequences not related to the SNARE proteins has not been accomplished yet; this is due, in part, to the structural constraints and the specificity of the protein interactions that govern the formation of the SNARE complex. Here we have addressed this question and used a combinatorial approach to identify peptides that modulate the assembly of the SNARE core complex and inhibit neuronal…

Models MolecularVesicle fusionMacromolecular SubstancesChromaffin CellsMolecular Sequence DataVesicular Transport ProteinsBiologyBiochemistryExocytosisExocytosisProtein Structure SecondaryPeptide LibraryAnimalsAmino Acid SequencePeptide libraryMolecular BiologyCells CulturedSNARE complex assemblyNeuronsSTX1AMembrane ProteinsMunc-18Cell BiologyFusion proteinCell biologyRatsCattleSNARE complexPeptidesSNARE ProteinsResearch ArticleThe Biochemical journal
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Molecular and topological membrane folding determinants of transient receptor potential vanilloid 2 channel.

2015

Transient Receptor Potential (TRP) channels are related to adaptation to the environment and somatosensation. The transient receptor potential vanilloid (TRPV) subfamily includes six closely evolutionary related ion channels sharing the same domain organization and tetrameric arrangement in the membrane. In this study we have characterized biochemically TRPV2 channel membrane protein folding and transmembrane (TM) architecture. Deleting the first N-terminal 74 residues preceding the ankyrin repeat domain (ARD) show a key role for this region in targeting the protein to the membrane. We have demonstrated the co-translational insertion of the membrane-embedded region of the TRPV2 and its disp…

Models MolecularVesicle-associated membrane protein 8Protein FoldingTRPV5Protein ConformationBiophysicsTRPV Cation ChannelsBiochemistryTRPVTransient receptor potential channelAnimalsHumansProtein Structure QuaternaryMolecular BiologyIon channelTransmembrane channelsChemistryCell MembraneCell BiologyTransmembrane proteinRecombinant ProteinsAnkyrin RepeatProtein Structure TertiaryRatsHEK293 CellsBiochemistryBiophysicsAnkyrin repeatBiochemical and biophysical research communications
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Oligomerization of polytopic α-helical membrane proteins: causes and consequences

2012

Abstract Several polytopic α-helical membrane-integrated proteins appear to be organized in higher-ordered oligomeric complexes. While many aspects are still enigmatic, in recent years, the physiological impact of membrane protein oligomerization has been analyzed to some extent. In the present article, oligomerization of structurally well-defined membrane proteins is discussed. The available experimental information indicates the causes and physiological consequences of membrane protein oligomerization, including stabilization, cooperative functions, and control of specific activities. Based on the currently available observations, we aim to derive some general principles and discuss open …

Models MolecularVesicle-associated membrane protein 8Protein StabilityChemistryClinical BiochemistryPeripheral membrane proteinMembrane ProteinsBiochemistryProtein Structure SecondaryMembrane proteinBiochemistryα helicalBiophysicsHumansMolecular BiologyIntegral membrane proteinFunction (biology)G protein-coupled receptorbchm
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A molecular assembly system that renders antigens of choice highly repetitive for induction of protective B cell responses.

2002

Virus like particles (VLPs) are known to induce potent B cell responses in the absence of adjuvants. Moreover, epitope-specific antibody responses may be induced by VLPs that contain peptides inserted in their immunodominant regions. However, due to steric problems, the size of the peptides capable of being incorporated into VLPs while still permitting capsid assembly, is rather limited. While peptides genetically fused to either the N- or C-terminus of VLPs present fewer assembly problems, the immune responses obtained against such epitopes are often limited, most likely because the epitopes are not optimally exposed. In addition, such particles may be less stable in vivo. Here, we show th…

Models MolecularViral Hepatitis VaccinesHepatitis B virusMacromolecular SubstancesProtein ConformationvirusesRecombinant Fusion ProteinsProtozoan ProteinsAntigens ProtozoanBiologyProtein EngineeringEpitopePhospholipases AInclusion Bodies ViralViral Matrix ProteinsMiceImmune systemAntigenVirus-like particlemedicineAnimalsB cellB-LymphocytesMice Inbred BALB CVaccines SyntheticGeneral VeterinaryGeneral Immunology and MicrobiologyImmunodominant EpitopesImmunogenicityVaccinationPublic Health Environmental and Occupational HealthMolecular biologyHepatitis B Core AntigensPeptide FragmentsCell biologyProtein Structure TertiaryHBcAgBee VenomsInfectious Diseasesmedicine.anatomical_structureCross-Linking ReagentsCapsidDrug DesignMolecular MedicineFemaleImmunizationPeptidesOligopeptidesVaccine
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Insights into virus evolution and membrane biogenesis from the structure of the marine lipid-containing bacteriophage PM2.

2008

Recent, primarily structural observations indicate that related viruses, harboring no sequence similarity, infect hosts of different domains of life. One such clade of viruses, defined by common capsid architecture and coat protein fold, is the so-called PRD1-adenovirus lineage. Here we report the structure of the marine lipid-containing bacteriophage PM2 determined by crystallographic analyses of the entire approximately 45 MDa virion and of the outer coat proteins P1 and P2, revealing PM2 to be a primeval member of the PRD1-adenovirus lineage with an icosahedral shell and canonical double beta barrel major coat protein. The view of the lipid bilayer, richly decorated with membrane protein…

Models MolecularViral proteinProtein ConformationvirusesMolecular Sequence DataBiologymedicine.disease_causeCrystallography X-Ray03 medical and health sciencesProtein structuremedicineLipid bilayerMolecular Biology030304 developmental biology0303 health sciences030306 microbiologyCorticoviridaeVirionCell BiologyVirologyBiological EvolutionLipidsCell biologyBeta barrelMembrane proteinCapsidViral evolutionMembrane biogenesisVirusesCalciumCapsid ProteinsMolecular cell
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