Search results for "Structural Biology."

showing 10 items of 822 documents

Molecular dynamics simulation of sucrose- and trehalose-coated carboxy-myoglobin

2005

We performed a room temperature molecular dynamics (MD) simulation on a system containing 1 carboxy-myoglobin (MbCO) molecule in a sucrose–water matrix of identical composition (89% [sucrose/(sucrose + water)] w/w) as for a previous trehalose–water–MbCO simulation (Cottone et al., Biophys J 2001;80:931–938). Results show that, as for trehalose, the amplitude of protein atomic mean-square fluctuations, on the nanosecond timescale, is reduced with respect to aqueous solutions also in sucrose. A detailed comparison as a function of residue number evidences mobility differences along the protein backbone, which can be related to a different efficacy in bioprotection. Different heme pocket struc…

Models MolecularInfrared spectroscopyDisaccharidesBiochemistrychemistry.chemical_compoundMolecular dynamicsStructural BiologyCarbohydrate ConformationMoleculeComputer Simulationheme pocket; hydrogen bond; mean-square fluctuations; protein dynamics; sucrose; trehaloseheme pocketMolecular Biologytrehalosehydrogen bondAqueous solutionBinding SitesHydrogen bondMyoglobinProtein dynamicssucroseTrehaloseCrystallographyKineticschemistryMyoglobinprotein dynamicsmolecular dynamics myoglobin disaccharidemean-square fluctuations
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Modulation of lipid-induced ER stress by fatty acid shape.

2011

IF : 5,709; International audience; Exposure of pancreatic β cells to long-chain saturated fatty acids (SFA) induces a so-called endoplasmic reticulum (ER) stress that can ultimately lead to cell death. This process is believed to participate in insulin deficiency associated with type 2 diabetes, via a decrease in β-cell mass. By contrast, some unsaturated fatty acid species appear less toxic to the cells and can even alleviate SFA-induced ER stress. In the present study, we took advantage of a simple yeast-based model, which brings together most of the trademarks of lipotoxicity in human cells, to screen fatty acids of various structures for their capacity to counter ER stress. Here we dem…

Models MolecularLipid Bilayers[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Endoplasmic ReticulumBiochemistry03 medical and health sciences0302 clinical medicine[ SDV.BBM.BC ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]Structural BiologyStress PhysiologicalGeneticsHumansadipocyte protein 2[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Molecular BiologyUnsaturated fatty acidCells CulturedPhospholipids030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyEndoplasmic reticulumFatty Acids[ SDV.BC.BC ] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]food and beveragesFatty acidCell BiologyLipidsCell biologychemistryLipotoxicityFree fatty acid receptorUnfolded protein responsebiology.proteinFatty Acids Unsaturated030217 neurology & neurosurgeryPolyunsaturated fatty acid
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Crystal structure of the N-terminal domain of the major virulence factor BB0323 from the Lyme disease agent Borrelia burgdorferi.

2019

Lyme disease is an infection caused by the spirochete Borrelia burgdorferi after it is transmitted to a mammalian organism during a tick blood meal. B. burgdorferi encodes at least 140 lipoproteins located on the outer or inner membrane, thus facing the surroundings or the periplasmic space, respectively. However, most of the predicted lipoproteins are of unknown function, and only a few proteins are known to be essential for the persistence and virulence of the pathogen. One such protein is the periplasmic BB0323, which is indispensable for B. burgdorferi to cause Lyme disease and the function of which is associated with cell fission and outer membrane integrity. After expression and trans…

Models MolecularLyme DiseaseVirulence FactorsLipoproteinsVirulencePeriplasmic spaceBiologybiology.organism_classificationVirulence factorCell biologyBacterial ProteinsStructural BiologyBorrelia burgdorferiInner membraneSpectrinAmino Acid SequenceBorrelia burgdorferiBacterial outer membranePathogenActa crystallographica. Section D, Structural biology
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High-resolution solution NMR structure of the Z domain of staphylococcal protein A

1997

Staphylococcal protein A (SpA) is a cell-wall-bound pathogenicity factor from the bacterium Staphylococcus aureus. Because of their small size and immunoglobulin (IgG)-binding activities, domains of protein A are targets for protein engineering efforts and for the development of computational approaches for de novo protein folding. The NMR solution structure of an engineered IgG-binding domain of SpA, the Z domain (an analog of the B domain of SpA), has been determined by simulated annealing with restrained molecular dynamics on the basis of 671 conformational constraints. The Z domain contains three well-defined alpha-helices corresponding to polypeptide segments Lys7 to Leu17 (helix 1), G…

Models MolecularMagnetic Resonance SpectroscopyProtein ConformationChemistryMolecular Sequence DataProtein engineeringHydrogen-Ion ConcentrationCrystallography X-RayAntiparallel (biochemistry)CrystallographyModels ChemicalStructural BiologyHelixHumansHydrogen–deuterium exchangeAmino Acid SequenceB3 domainStaphylococcal Protein AMolecular BiologyTwo-dimensional nuclear magnetic resonance spectroscopyConformational isomerismHeteronuclear single quantum coherence spectroscopyJournal of Molecular Biology
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Formation, TEM study and 3D reconstruction of the human erythrocyte peroxiredoxin-2 dodecahedral higher-order assembly.

2004

The production of a higher-order assembly of peroxiredoxin-2 (Prx-2) from human erythrocytes has been achieved during specimen preparation on holey carbon support films, in the presence of ammonium molybdate and polyethylene glycol. TEM study suggested that this assembly is a regular dodecahedron, containing 12 Prx-2 decamers (Mr 2.62 MDa, external diameter approximately 20 nm). This interpretation has been supported by production of a approximately 1.6 nm 3D reconstruction from the negative stain TEM data, with automated docking of the available X-ray data of the Prx-2 decamer. Comparison with other known protein dodecahedral and viral icosahedral structures indicates that this arrangement…

Models MolecularMaterials scienceErythrocytesIcosahedral symmetryMacromolecular SubstancesMacromolecular SubstancesGeneral Physics and AstronomyCell BiologyPeroxiredoxin 2Polyethylene glycolPeroxiredoxinsNegative stainDodecahedronCrystallographychemistry.chemical_compoundProtein structurechemistryMicroscopy Electron TransmissionPeroxidasesStructural BiologyImage Processing Computer-AssistedHumansGeneral Materials ScienceProtein Structure QuaternaryMacromoleculeMicron (Oxford, England : 1993)
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3-Chlorotyramine Acting as Ligand of the D2 Dopamine Receptor. Molecular Modeling, Synthesis and D2 Receptor Affinity.

2014

We synthesized and tested 3-chlorotyramine as a ligand of the D2 dopamine receptor. This compound displayed a similar affinity by this receptor to that previously reported for dopamine. In order to understand further the experimental results we performed a molecular modeling study of 3-chlorotyramine and structurally related compounds. By combining molecular dynamics simulations with semiempirical (PM6), ab initio and density functional theory calculations, a simple and generally applicable procedure to evaluate the binding energies of these ligands interacting with the D2 dopamine receptors is reported here. These results provided a clear picture of the binding interactions of these compou…

Models MolecularMolecular modelChemistryReceptors Dopamine D2Organic ChemistryBinding energyAtoms in moleculesAb initioTyramineComputer Science ApplicationsMolecular dynamicsDopamine D2 Receptor AntagonistsStructural BiologyDopamine receptorComputational chemistryDopamine receptor D2Drug DiscoveryHydrocarbons ChlorinatedMolecular MedicineHumansDensity functional theoryMolecular informatics
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Limulus polyphemus Hemocyanin: 10 Å Cryo-EM Structure, Sequence Analysis, Molecular Modelling and Rigid-body Fitting Reveal the Interfaces Between th…

2007

Abstract The blue copper protein hemocyanin from the horseshoe crab Limulus polyphemus is among the largest respiratory proteins found in nature (3.5 MDa) and exhibits a highly cooperative oxygen binding. Its 48 subunits are arranged as eight hexamers (1×6mers) that form the native 8×6mer in a nested hierarchy of 2×6mers and 4×6mers. This quaternary structure is established by eight subunit types (termed I, IIA, II, IIIA, IIIB, IV, V, and VI), of which only type II has been sequenced. Crystal structures of the 1×6mer are available, but for the 8×6mer only a 40 A 3D reconstruction exists. Consequently, the structural parameters of the 8×6mer are not firmly established, and the molecular inte…

Models MolecularMolecular modelCryo-electron microscopyCopper proteinProtein subunitmedicine.medical_treatmentMolecular Sequence DataStructure-Activity RelationshipStructural BiologyHorseshoe CrabsmedicineAnimalsAmino Acid SequenceProtein Structure QuaternaryMolecular BiologyPhylogenySequence Homology Amino AcidbiologyCryoelectron MicroscopyHemocyaninbiology.organism_classificationProtein Structure TertiaryCrystallographyLimulusHemocyaninsProtein quaternary structureOxygen bindingJournal of Molecular Biology
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Nautilus pompilius Hemocyanin: 9 Å Cryo-EM Structure and Molecular Model Reveal the Subunit Pathway and the Interfaces between the 70 Functional Units

2007

Hemocyanins are giant extracellular oxygen carriers in the hemolymph of many molluscs. Nautilus pompilius (Cephalopoda) hemocyanin is a cylindrical decamer of a 350 kDa polypeptide subunit that in turn is a "pearl-chain" of seven different functional units (FU-a to FU-g). Each globular FU has a binuclear copper centre that reversibly binds one O(2) molecule, and the 70-FU decamer is a highly allosteric protein. Its primary structure and an 11 A cryo-electron microscopy (cryo-EM) structure have recently been determined, and the crystal structures of two related FU types are available in the databanks. However, in molluscan hemocyanin, the precise subunit pathway within the decamer, the inter…

Models MolecularMolecular modelProtein Conformationmedicine.medical_treatmentProtein subunitMolecular Sequence DataOctopodiformesAllosteric regulationBiologyHemocyaninTurn (biochemistry)Protein structureStructural BiologyImage Processing Computer-AssistedmedicineAnimalsAmino Acid SequenceMolecular BiologyBinding SitesSequence Homology Amino AcidCryoelectron MicroscopyProtein primary structureHemocyaninCrystallographyHemocyaninsBiophysicsNautilusProtein quaternary structureJournal of Molecular Biology
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Keyhole limpet hemocyanin: 9-A CryoEM structure and molecular model of the KLH1 didecamer reveal the interfaces and intricate topology of the 160 fun…

2008

Abstract Hemocyanins are blue copper-containing respiratory proteins in the hemolymph of many arthropods and molluscs. Molluscan hemocyanins are decamers, didecamers, or multidecamers of a 340- to 400-kDa polypeptide subunit containing seven or eight globular functional units (FUs; FU-a to FU-h), each with an oxygen-binding site. The decamers are short 35-nm hollow cylinders, with their lumen narrowed by a collar complex. Our recently published 9-A cryo-electron microscopy/crystal structure hybrid model of a 3.4-MDa cephalopod hemocyanin decamer [Nautilus pompilius hemocyanin (NpH)] revealed the pathway of the seven-FU subunit (340 kDa), 15 types of inter-FU interface, and an asymmetric col…

Models MolecularMolecular modelbiologySequence Homology Amino AcidCryo-electron microscopyProtein subunitmedicine.medical_treatmentCryoelectron MicroscopyMolecular Sequence DataOxygen transportHemocyaninCrystallographyBiopolymersStructural BiologyHemolymphHemocyaninsmedicinebiology.proteinAnimalsProtein quaternary structureAmino Acid SequenceMolecular BiologyKeyhole limpet hemocyaninJournal of molecular biology
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10-A cryoEM structure and molecular model of the Myriapod (Scutigera) 6x6mer hemocyanin:understanding a giant oxygen transport protein

2009

Oxygen transport in Myriapoda is maintained by a unique 6x6mer hemocyanin, that is, 36 subunits arranged as six hexamers (1x6mers). In the sluggish diplopod Spirostreptus, the 1x6mers seem to operate as almost or fully independent allosteric units (h approximately 1.3; P(50) approximately 5 torr), whereas in the swift centipede Scutigera, they intensively cooperate allosterically (h approximately 10; P(50) approximately 50 torr). Here, we show the chemomechanical basis of this differential behavior as deduced from hybrid 6x6mer structures, obtained by single-particle cryo-electron microscopy of the Scutigera 6x6mer (10.0 A resolution according to the 0.5 criterion) and docking of homology-m…

Models MolecularMolecular modelmedicine.medical_treatmentProtein subunitMolecular Sequence DataProtein Data Bank (RCSB PDB)Hemocyaninchemistry.chemical_compoundStructural BiologymedicineAnimalsCarboxylateAmino Acid SequenceProtein Structure QuaternaryMolecular BiologyHistidinebiologyCryoelectron MicroscopyOxygen transportHemocyaninSpirostreptusbiology.organism_classificationOxygenCrystallographychemistryHemocyaninsProtein MultimerizationCarrier ProteinsSequence Alignment
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