Search results for "Protein Structure"

showing 7 items of 757 documents

Thyroid hormones induce sumoylation of the cold shock domain-containing protein PIPPin in developing rat brain and in cultured neurons.

2006

We previously identified a cold shock domain (CSD)-containing protein (PIPPin), expressed at high level in brain cells. PIPPin has the potential to undergo different post-translational modifications and might be a good candidate to regulate the synthesis of specific proteins in response to extracellular stimuli. Here we report the effects of thyroid hormone (T3) on PIPPin expression in developing rat brain. We found that a significant difference among euthyroid- and hypothyroid- newborn rats concerns sumoylation of nuclear PIPPin, that is abolished by hypothyroidism. Moreover, T3-dependence of PIPPin sumoylation has been confirmed in cortical neurons purified from brain cortices and culture…

medicine.medical_specialtySUMO-1 ProteinSUMO proteinDeveloping rat brainNerve Tissue ProteinsEndocrinologyAntithyroid AgentsHypothyroidismPregnancyInternal medicinemedicineExtracellularAnimalsRats WistarCells CulturedCell NucleusCerebral CortexNeuronsbiologyRNA-Binding ProteinsCold-shock domainChromatinProtein Structure TertiaryRatsThyroid hormoneChemically defined mediumCell nucleusmedicine.anatomical_structureHistoneEndocrinologyAnimals NewbornPropylthiouracilPrenatal Exposure Delayed Effectsbiology.proteinTriiodothyronineRNA-binding proteins (RBPs)FemaleRabbitsNucleusEndocrinology
researchProduct

Multiphoton Absorption of Myoglobin Nitric-Oxide complex: Relaxation by D-NEMD of a Stationary State

2012

ABSTRACT: The photodissociation and geminate recombination of nitric oxide in myoglobin, under continuous illumination, is modeled computationally. The relaxation of the photon energy into the protein matrix is also considered in a single simulation scheme that mimics a complete experimental setup. The dynamic approach to non-equilibrium molecular dynamics is used, starting from a steady state, to compute its relaxation to equilibrium. Simulations are conducted for the native form of sperm whale myoglobin and for two other mutants, V68W and L29F, illustrating a fair diversity of spatial and temporal geminate recombination processes. Energy flow to the heme and immediate protein environment …

myoglobin molecular dynamics simulations non equilibriumThermal fluctuationsMolecular Dynamics SimulationNitric OxideArticleAbsorptionchemistry.chemical_compoundMolecular dynamicsComputational chemistryMaterials ChemistryPhysical and Theoretical ChemistryHemePhotonsSteady stateChemistryMyoglobinPhotodissociationTemperatureSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Recombinant ProteinsSurfaces Coatings and FilmsProtein Structure TertiaryMyoglobinChemical physicsMutationRelaxation (physics)Stationary stateProtein Binding
researchProduct

The Interconnecting Hairpin Extension "Arm": An Essential Allosteric Element of Phytochrome Activity

2023

In red-light sensing phytochromes, isomerization of the bilin chromophore triggers structural and dynamic changes across multiple domains, ultimately leading to control of the output module (OPM) activity. In between, a hairpin structure, "arm", extends from an interconnecting domain to the chromophore region. Here, by removing this protein segment in a bacteriophytochrome from Deinococcus radiodurans (DrBphP), we show that the arm is crucial for signal transduction. Crystallographic, spectroscopic, and biochemical data indicate that this variant maintains the properties of DrBphP in the resting state. Spectroscopic data also reveal that the armless systems maintain the ability to respond t…

phytochromesoluviestintäphotosensorallostery92-11histidine kinanasephotoreceptorthermal stabilityreseptorit (biokemia)87.1592-05structure and functionproteiinitvalokemia87.14 2000 MSCprotein structurePACSsignal transduction
researchProduct

Synthesis and Structure-Affinity Relationships of Spirocyclic Benzopyrans with Exocyclic Amino Moiety

2019

σ1 and/or σ2 receptors play a crucial role in pathological conditions such as pain, neurodegenerative disorders, and cancer. A set of spirocyclic cyclohexanes with diverse O-heterocycles and amino moieties (general structure III) was prepared and pharmacologically evaluated. In structure-activity relationships studies, the σ1 receptor affinity and σ1:σ2 selectivity were correlated with the stereochemistry, the kind and substitution pattern of the O-heterocycle, and the substituents at the exocyclic amino moiety. cis-configured 2-benzopyran cis-11b bearing a methoxy group and a tertiary cyclohexylmethylamino moiety showed the highest σ1 affinity ( Ki = 1.9 nM) of this series of compounds. In…

synthesisexocyclic amino moietyReceptors Opioid mudocking studieCrystallography X-RayLigands01 natural sciencesopioid receptorschemistry.chemical_compoundProtein structureDrug DiscoveryMoiety0303 health sciencesσ1 receptor ligandsstructure (σ1) affinity relationshipmolecular dynamicBenzyl groupMolecular MedicinesynthesiBenzopyransSelectivityHydrophobic and Hydrophilic Interactionsfree binding enthalpyStereochemistrychange of receptor profileMolecular Dynamics Simulation03 medical and health sciencesStructure-Activity Relationshipσ1 receptor ligands; spirocyclic compounds; benzopyrans; benzofurans; exocyclic amino moiety; synthesis; structure (σ1) affinity relationships; σ1 antagonistic activity; receptor selectivity; molecular dynamics; docking studies; free binding enthalpy; X-ray crystal structure; opioid receptors; MOR affinity; change of receptor profile; structure MOR affinity relationshipsstructure (σ1) affinity relationshipsStructure–activity relationshipHumansReceptors sigmaBenzopyransSpiro Compoundsspirocyclic compoundBinding siteMOR affinity030304 developmental biologybenzopyranbenzofuransσ1 receptor ligandBinding Sitesspirocyclic compoundsreceptor selectivitystructure MOR affinity relationshipsdocking studiesbenzofuranopioid receptorX-ray crystal structuremolecular dynamics0104 chemical sciencesProtein Structure Tertiary010404 medicinal & biomolecular chemistrychemistrySalt bridgeσ1 antagonistic activity
researchProduct

Eukaryotic rRNA Modification by Yeast 5-Methylcytosine-Methyltransferases and Human Proliferation-Associated Antigen p120.

2015

International audience; Modified nucleotide 5-methylcytosine (m(5)C) is frequently present in various eukaryotic RNAs, including tRNAs, rRNAs and in other non-coding RNAs, as well as in mRNAs. RNA: m(5)C-methyltranferases (MTases) Nop2 from S. cerevisiae and human proliferation-associated nucleolar antigen p120 are both members of a protein family called Nop2/NSUN/NOL1. Protein p120 is well-known as a tumor marker which is over-expressed in various cancer tissues. Using a combination of RNA bisulfite sequencing and HPLC-MS/MS analysis, we demonstrated here that p120 displays an RNA:m(5)C-MTase activity, which restores m(5)C formation at position 2870 in domain V of 25S rRNA in a nop2 Delta …

tRNA MethyltransferasesSaccharomyces cerevisiae Proteinslcsh:RNuclear Proteinslcsh:MedicineMethyltransferasesSaccharomyces cerevisiaeProtein Structure TertiaryRNA Ribosomal5-MethylcytosineHumans[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biologylcsh:Qlcsh:Science[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyProtein BindingResearch ArticlePLoS ONE
researchProduct

Lipid Binding Controls Dimerization of the Coat Protein p24 Transmembrane Helix

2019

Abstract Coat protein (COP) I and COP II complexes are involved in the transport of proteins between the endoplasmic reticulum and the Golgi apparatus in eukaryotic cells. The formation of COP I/II complexes at membrane surfaces is an early step in vesicle formation and is mastered by p24, a type I transmembrane protein. Oligomerization of p24 monomers was suggested to be mediated and/or stabilized via interactions within the transmembrane domain, and the p24 transmembrane helix appears to selectively bind a single sphingomyelin C18:0 molecule. Furthermore, a potential cholesterol-binding sequence has also been predicted in the p24 transmembrane domain. Thus, sphingomyelin and/or cholestero…

virusesLipid BilayersBiophysicsProtein Structure Secondary03 medical and health sciencessymbols.namesake0302 clinical medicineimmune system diseasesAmino Acid Sequence030304 developmental biology0303 health sciencesChemistryEndoplasmic reticulumVesicleCholesterol bindingvirus diseasesArticlesCOPIGolgi apparatusLipidsTransmembrane proteinSphingomyelinsTransmembrane domainCholesterolsymbolsBiophysicsCapsid Proteinslipids (amino acids peptides and proteins)SphingomyelinDimerization030217 neurology & neurosurgeryBiophysical Journal
researchProduct

The Extracellular δ-Domain is Essential for the Formation of CD81 Tetraspanin Webs

2014

AbstractCD81 is a ubiquitously expressed member of the tetraspanin family. It forms large molecular platforms, so-called tetraspanin webs that play physiological roles in a variety of cellular functions and are involved in viral and parasite infections. We have investigated which part of the CD81 molecule is required for the formation of domains in the cell membranes of T-cells and hepatocytes. Surprisingly, we find that large CD81 platforms assemble via the short extracellular δ-domain, independent from a strong primary partner binding and from weak interactions mediated by palmitoylation. The δ-domain is also essential for the platforms to function during viral entry. We propose that, ins…

virusesLipoylationBiophysicschemical and pharmacologic phenomenaPlasma protein bindingBiologyTetraspanin 28Jurkat CellsProtein structurePalmitoylationTetraspaninViral entryExtracellularHumansComputingMilieux_MISCELLANEOUS[PHYS]Physics [physics]MembranesHep G2 Cellsbiochemical phenomena metabolism and nutritionCell biologyProtein Structure TertiaryProtein MultimerizationProtein Processing Post-TranslationalFunction (biology)CD81Protein Binding
researchProduct