Search results for "binding sites"

showing 10 items of 636 documents

The hydrolysis of 6-phosphogluconolactone in the second step of pentose phosphate pathway occurs via a two-water mechanism.

2018

Hydrolysis reaction marks the basis of life yet the mechanism of this crucial biochemical reaction is not completely understood. We recently reported the mechanisms of hydrolysis of nucleoside triphosphate and phosphate monoester. These two reactions hydrolyze P-O-P and P-O-C linkages, respectively. Here, we present the mechanism of hydrolysis of δ-6-phosphogluconolactone, which is an important precursor in the second step of the pentose phosphate pathway. Its hydrolysis requires the cleavage of C-O-C linkage and its mechanism is hitherto unknown. We report three mechanisms of hydrolysis of δ-6-phosphogluconolactone based on density functional computations. In the energetically most favorab…

0301 basic medicineModels MolecularStereochemistryBiophysicsPentose phosphate pathway010402 general chemistryCleavage (embryo)01 natural sciencesBiochemistryGluconatesPentose Phosphate Pathway03 medical and health scienceschemistry.chemical_compoundHydrolysis6-Phosphogluconolactonechemistry.chemical_classificationBinding SitesHydrolysisOrganic ChemistryWaterPhosphate0104 chemical sciencesEcoRV030104 developmental biologyEnzymechemistryNucleoside triphosphateQuantum TheoryThermodynamicsBiophysical chemistry
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Coordination of the biliverdin D-ring in bacteriophytochromes.

2018

Phytochrome proteins translate light into biochemical signals in plants, fungi and microorganisms. Light cues are absorbed by a bilin chromophore, leading to an isomerization and a rotation of the D-ring. This relays the signal to the protein matrix. A set of amino acids, which is conserved across the phytochrome superfamily, holds the chromophore in the binding pocket. However, the functional role of many of these amino acids is not yet understood. Here, we investigate the hydrogen bonding network which surrounds the D-ring of the chromophore in the resting (Pr) state. We use UV/vis spectroscopy, infrared absorption spectroscopy and X-ray crystallography to compare the photosensory domains…

0301 basic medicineModels MolecularStereochemistryProtein ConformationProtein Data Bank (RCSB PDB)General Physics and Astronomyphytochrome proteinsbakteerit03 medical and health scienceschemistry.chemical_compoundProtein structureBacterial ProteinsProteobacteriabiochemical signalsDeinococcusPhysical and Theoretical ChemistryStigmatella aurantiacaBiliverdinBinding SitesbiologyPhytochromeBiliverdineta1182Deinococcus radioduransHydrogen BondingChromophorebiology.organism_classificationPhotochemical ProcessesD-ring030104 developmental biologychemistryproteiinitvalokemiaDeinococcusPhytochromeProtein BindingPhysical chemistry chemical physics : PCCP
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eIF5A facilitates translation termination globally and promotes the elongation of many non polyproline-specific tripeptide sequences

2017

Abstract eIF5A is an essential protein involved in protein synthesis, cell proliferation and animal development. High eIF5A expression is observed in many tumor types and has been linked to cancer metastasis. Recent studies have shown that eIF5A facilitates the translation elongation of stretches of consecutive prolines. Activated eIF5A binds to the empty E-site of stalled ribosomes, where it is thought to interact with the peptidyl-tRNA situated at the P-site. Here, we report a genome-wide analysis of ribosome stalling in Saccharomyces cerevisiae eIF5A depleted cells using 5Pseq. We confirm that, in the absence of eIF5A, ribosomes stall at proline stretches, and extend previous studies by …

0301 basic medicinePeptidyl transferaseProlineCytoskeleton organizationAmino Acid MotifsSaccharomyces cerevisiaePeptide Chain Elongation TranslationalSaccharomyces cerevisiaeBioinformaticsRibosomeGTP Phosphohydrolases03 medical and health sciences0302 clinical medicinePeptide Initiation FactorsGene Expression Regulation FungalGeneticsProtein biosynthesisHumansMolecular BiologyPolyproline helixBinding SitesbiologyRNA-Binding Proteinsbiology.organism_classificationStop codonCell biology030104 developmental biologybiology.proteinGenome FungalHydrophobic and Hydrophilic InteractionsRibosomesEIF5A030217 neurology & neurosurgeryProtein BindingNucleic Acids Research
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Ultrafast structural changes within a photosynthetic reaction centre

2021

Nature <London> / Physical science 589, 310 - 314 (2021). doi:10.1038/s41586-020-3000-7

0301 basic medicinePhotosynthetic reaction centreChlorophyllModels MolecularklorofylliCytoplasmUbiquinonePhotosynthetic Reaction Center Complex ProteinsElectrons02 engineering and technologyPhotochemistrymedicine.disease_cause530yhteyttäminenbakteeritElectron Transport03 medical and health sciencesElectron transfermedicineMoleculeddc:530BacteriochlorophyllsbioenergetiikkaComputingMilieux_MISCELLANEOUSHyphomicrobiaceaeMultidisciplinaryBinding SitesCrystallography[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]ChemistryBlastochloris viridisLaserskalvot (biologia)PheophytinsBiological membraneVitamin K 2021001 nanoscience & nanotechnologyAcceptor030104 developmental biologyPicosecondFemtosecondsense organsProtons0210 nano-technologyOxidation-Reductionröntgenkristallografia
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A Peptidoglycan-Remodeling Enzyme Is Critical for Bacteroid Differentiation in Bradyrhizobium spp. During Legume Symbiosis.

2016

International audience; In response to the presence of compatible rhizobium bacteria, legumes form symbiotic organs called nodules on their roots. These nodules house nitrogen-fixing bacteroids that are a differentiated form of the rhizobium bacteria. In some legumes, the bacteroid differentiation comprises a dramatic cell enlargement, polyploidization, and other morphological changes. Here, we demonstrate that a peptidoglycan-modifying enzyme in Bradyrhizobium strains, a DD-carboxypeptidase that contains a peptidoglycan-binding SPOR domain, is essential for normal bacteroid differentiation in Aeschynomene species. The corresponding mutants formed bacteroids that are malformed and hypertrop…

0301 basic medicinePhysiology[SDV]Life Sciences [q-bio]Mutantnodosité racinairechemistry.chemical_compoundBacteroidesBradyrhizobiumPhotosynthesisPhotosynthèseDifférenciation cellulaire2. Zero hungerhttp://aims.fao.org/aos/agrovoc/c_2603http://aims.fao.org/aos/agrovoc/c_6094food and beveragesFabaceaeGeneral MedicinePolyploïdieCode génétiqueRhizobiumhttp://aims.fao.org/aos/agrovoc/c_3215Symbiosihttp://aims.fao.org/aos/agrovoc/c_27138F60 - Physiologie et biochimie végétaleSymbioseBacterial Proteinhttp://aims.fao.org/aos/agrovoc/c_772PeptidoglycanBiologyBradyrhizobiumMicrobiology03 medical and health sciencesPhotosynthesiBacterial ProteinsSymbiosisPeptidaseSymbiosishttp://aims.fao.org/aos/agrovoc/c_7563Binding Sites[ SDV ] Life Sciences [q-bio]Binding SiteP34 - Biologie du solAeschynomeneGene Expression Regulation Bacterialbiology.organism_classificationhttp://aims.fao.org/aos/agrovoc/c_27601http://aims.fao.org/aos/agrovoc/c_5014030104 developmental biologychemistryEnzymeMutationhttp://aims.fao.org/aos/agrovoc/c_5812http://aims.fao.org/aos/agrovoc/c_5690PeptidoglycanBacteroidesAgronomy and Crop ScienceBacteriahttp://aims.fao.org/aos/agrovoc/c_2265
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Prospective Evaluation of Free Energy Calculations for the Prioritization of Cathepsin L Inhibitors.

2017

Improving the binding affinity of a chemical series by systematically probing one of its exit vectors is a medicinal chemistry activity that can benefit from molecular modeling input. Herein, we compare the effectiveness of four approaches in prioritizing building blocks with better potency: selection by a medicinal chemist, manual modeling, docking followed by manual filtering, and free energy calculations (FEP). Our study focused on identifying novel substituents for the apolar S2 pocket of cathepsin L and was conducted entirely in a prospective manner with synthesis and activity determination of 36 novel compounds. We found that FEP selected compounds with improved affinity for 8 out of …

0301 basic medicinePrioritizationMolecular modelHalogenationStereochemistryCathepsin LComputational biology01 natural sciencesMolecular Docking SimulationProspective evaluationCathepsin L03 medical and health sciences0103 physical sciencesDrug DiscoveryHumansEnzyme InhibitorsBinding Sites010304 chemical physicsbiologyChemistryMolecular Docking Simulation030104 developmental biologyPyrimidinesDocking (molecular)Drug Designbiology.proteinMolecular MedicineThermodynamicsProtein BindingJournal of medicinal chemistry
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The C-terminal region of human plasma fetuin-B is dispensable for the raised-elephant-trunk mechanism of inhibition of astacin metallopeptidases

2019

© The Author(s) 2019.

0301 basic medicineProteasesProtein Conformationlcsh:MedicineAstacoideaCrystallography X-RayCleavage (embryo)Protein Structure SecondaryArticleMice03 medical and health sciencesScissile bondHydrolaseAnimalsHumansAmino Acid Sequencelcsh:ScienceProtein secondary structureX-ray crystallographyBinding SitesMultidisciplinary030102 biochemistry & molecular biologyChemistrylcsh:RMetalloendopeptidasesProteasesFetuinFetuin-BCell biologyZincFertility030104 developmental biologyProteolysisMetalloproteaseslcsh:QAstacinLinkerScientific Reports
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Searching for Chymase Inhibitors among Chamomile Compounds Using a Computational-Based Approach

2018

Inhibitors of chymase have good potential to provide a novel therapeutic approach for the treatment of cardiovascular diseases. We used a computational approach based on pharmacophore modeling, docking, and molecular dynamics simulations to evaluate the potential ability of 13 natural compounds from chamomile extracts to bind chymase enzyme. The results indicated that some chamomile compounds can bind to the active site of human chymase. In particular, chlorogenic acid had a predicted binding energy comparable or even better than that of some known chymase inhibitors, interacted stably with key amino acids in the chymase active site, and appeared to be more selective for chymase than other …

0301 basic medicineProteaseschlorogenic acidlcsh:QR1-502030204 cardiovascular system & hematologyMolecular Dynamics SimulationCrystallography X-RayLigandsBiochemistrylcsh:MicrobiologyArticleSerine03 medical and health sciences0302 clinical medicineChymasesCatalytic DomainHumanschamomilecardiovascular diseases; chamomile; chlorogenic acid; chymase; docking; matricin; molecular dynamics simulations; pharmacophore; Biochemistry; Molecular BiologyEnzyme InhibitorsMolecular Biologychymasechemistry.chemical_classificationBinding SitesbiologypharmacophoreChymaseActive sitemolecular dynamics simulationsmatricinAmino acidcardiovascular diseasesMolecular Docking Simulation030104 developmental biologyEnzymechemistryBiochemistryDocking (molecular)dockingbiology.proteinPharmacophoreBiomolecules
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Evaluating the stability of pharmacophore features using molecular dynamics simulations.

2016

Abstract Molecular dynamics simulations of twelve protein—ligand systems were used to derive a single, structure based pharmacophore model for each system. These merged models combine the information from the initial experimental structure and from all snapshots saved during the simulation. We compared the merged pharmacophore models with the corresponding PDB pharmacophore models, i.e., the static models generated from an experimental structure in the usual manner. The frequency of individual features, of feature types and the occurrence of features not present in the static model derived from the experimental structure were analyzed. We observed both pharmacophore features not visible in …

0301 basic medicineProtein FlexibilityProtein ConformationBiophysicsStability (learning theory)Molecular Dynamics SimulationLigands01 natural sciencesBiochemistryLigandScoutSet (abstract data type)03 medical and health sciencesMolecular dynamicsComputational chemistryFeature (machine learning)Pharmacophore ModelingSensitivity (control systems)Molecular BiologyBinding Sites010405 organic chemistryChemistryStructure-based Pharmacophore ModelingMolecular DynamicProteinsHydrogen BondingCell Biology0104 chemical sciences030104 developmental biologyRankingModels ChemicalDrug DesignPharmacophoreBiological systemProtein BindingBiochemical and biophysical research communications
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Mechanism and biological role of Dnmt2 in Nucleic Acid Methylation

2016

ABSTRACT A group of homologous nucleic acid modification enzymes called Dnmt2, Trdmt1, Pmt1, DnmA, and Ehmet in different model organisms catalyze the transfer of a methyl group from the cofactor S-adenosyl-methionine (SAM) to the carbon-5 of cytosine residues. Originally considered as DNA MTases, these enzymes were shown to be tRNA methyltransferases about a decade ago. Between the presumed involvement in DNA modification-related epigenetics, and the recent foray into the RNA modification field, significant progress has characterized Dnmt2-related research. Here, we review this progress in its diverse facets including molecular evolution, structural biology, biochemistry, chemical biology,…

0301 basic medicineRetroelementsRNA methylationChemical biologyReviewBiologyMethylationCatalysisEpigenesis GeneticSubstrate Specificity03 medical and health scienceschemistry.chemical_compoundStructure-Activity RelationshipNucleic AcidsAnimalsHumansEpigeneticsDNA (Cytosine-5-)-MethyltransferasesGene SilencingMolecular BiologytRNAPhylogenyGeneticsNucleic acid methylationDNA methylationBinding SitesepigeneticsCell BiologyTRNA Methyltransferasesmethylcytidine030104 developmental biologyCell Transformation NeoplasticBiochemistrychemistryStructural biologyGene Expression RegulationNucleic acidRNA methylationDNAProtein BindingRNA Biology
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