Search results for "Structural homology"

showing 10 items of 14 documents

Structure-Activity Relationships of Cytotoxic Lactones as Inhibitors and Mechanisms of Action.

2020

Background: Some lactones prevent protein Myb-dependent gene expression. Objective: The object is to calculate inhibitors of Myb-brought genetic manifestation. Methods: Linear quantitative structure–potency relations result expanded, among sesquiterpene lactones of a variety of macrocycles (pseudoguaianolides, guaianolides, eudesmanolides and germacranolides), to establish which part of the molecule constitutes their pharmacophore, and predict their inhibitory potency on Myb-reliant genetic manifestation, which may result helpful as leads for antileukaemic therapies with a new mechanism of action. Results: Several count indices are connected with structure–activity. The α-methylene-γ-lacto…

0301 basic medicineGermacranolidePaclitaxelStereochemistrySesquiterpeneRing (chemistry)Ligands030226 pharmacology & pharmacy03 medical and health scienceschemistry.chemical_compoundLactonesStructure-Activity Relationship0302 clinical medicineTubulinNeoplasmsDrug DiscoverymedicinePotencyMoleculeHumansEtoposidechemistry.chemical_classification030102 biochemistry & molecular biologyAntineoplastic Agents PhytogenicTubulin ModulatorsMolecular Docking SimulationMechanism of actionchemistryStructural Homology ProteinDrug DesignPharmacophoremedicine.symptomTopotecanSesquiterpenesLactoneCurrent drug discovery technologies
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The inhibition of glycerol permeation through aquaglyceroporin-3 induced by mercury(II)

2016

Mercurial compounds are known to inhibit water permeation through aquaporins (AQPs). Although in the last years some hypotheses were proposed, the exact mechanism of inhibition is still an open question and even less is known about the inhibition of the glycerol permeation through aquaglyceroporins. Molecular dynamics (MD) simulations of human aquaporin-3 (AQP3) have been performed up to 200 ns in the presence of Hg2+ ions. For the first time, we have observed the unbiased passage of a glycerol molecule from the extracellular to cytosolic side. Moreover, the presence of Hg2+ ions covalently bound to Cys40 leads to a collapse of the aromatic/arginine selectivity filter (ar/R SF), blocking th…

Glycerol0301 basic medicineMolecular dynamicCell Membrane PermeabilityBiochemistryProtein Structure Secondarychemistry.chemical_compoundGLPFCOORDINATIONCRYSTALEscherichia coli ProteinsPermeationBiochemistryCovalent bondSettore CHIM/03 - Chimica Generale E InorganicaPhosphatidylcholinesCOMPLEXESProtein BindingSTRUCTURAL BASISCations DivalentPlasmodium falciparumAquaporinCYSTEINE-189Molecular Dynamics SimulationMolecular dynamicsAquaporinsWATER CHANNELInorganic Chemistry03 medical and health sciencesEscherichia coliGlycerolExtracellularHumansMoleculePERMEABILITYProtein Structure QuaternaryAquaporin 3Binding SitesAQUAPORIN INHIBITIONWaterBiological TransportMembranes ArtificialAquaglyceroporinMercurySIMULATIONSProtein Structure TertiaryCytosolWater permeation030104 developmental biologyAquaglyceroporinschemistryStructural Homology ProteinBiophysicsGlycerol permeationJournal of Inorganic Biochemistry
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Elevated blood Hsp60, its structural similarities and cross-reactivity with thyroid molecules, and its presence on the plasma membrane of oncocytes p…

2014

The role Hsp60 might play in various inflammatory and autoimmune diseases is under investigation, but little information exists pertaining to Hashimoto’s thyroiditis (HT). With the aim to fill this gap, in the present work, we directed our attention to Hsp60 participation in HT pathogenesis. We found Hsp60 levels increased in the blood of HT patients compared to controls. The chaperonin was immunolocalized in thyroid tissue specimens from patients with HT, both in thyrocytes and oncocytes (Hurthle cells) with higher levels compared to controls (goiter). In oncocytes, we found Hsp60 not only in the cytoplasm but also on the plasma membrane, as shown by double immunofluorescence performed on …

MaleIntegrinsmedicine.medical_treatmentThyroid Glandmedicine.disease_causeBiochemistryThyroiditisAutoimmunityHashimoto DiseaseThyroglobulin (TG)Hashimoto's thyroiditis (HT)Oxyphil CellsbiologyThyroid peroxidase (TPO)GoiterThyroidHsp60Immunohistochemistrymedicine.anatomical_structureFemaleAntibodyAdultmedicine.medical_specialtyendocrine systemanimal structuresMolecular Sequence Datachemical and pharmacologic phenomenaEnzyme-Linked Immunosorbent AssayHashimoto DiseaseCross Reactionscomplex mixturesIodide PeroxidaseThyroglobulinMitochondrial ProteinsYoung AdultThyroid peroxidaseInternal medicinemedicineHumansAmino Acid SequenceAutoantibodiesOriginal PaperfungiCell MembraneAutoantibodyComputational BiologyCell BiologyChaperonin 60medicine.diseaseHsp60 . Hashimoto's thyroiditis (HT) . Thyroglobulin (TG) . Thyroid peroxidase (TPO) . Autoantibodies . Oncocytes . Hurthle cells . Thyrocytes . Chaperonin . AutoimmunityEndocrinologyStructural Homology Proteinbiology.proteinLeukocytes MononuclearThyroglobulinCell stresschaperones
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Evolutionary conservation of the structural, pharmacological, and genomic characteristics of the melanocortin receptor subtypes

2005

We have cloned melanocortin receptors (MCRs) from several species of fish. The MC4R and MC5R subtypes arose early in vertebrate evolution and their primary structure is remarkably conserved. Expression and pharmacological characterization of the MCRs in fish has revealed that they bind and respond to melanocortin peptides with high potency. Detailed characterization of the binding properties of the different subtypes suggests that MCRs in early vertebrates had preference for adrenocorticotropic hormone (ACTH) peptides, while the high sensitivity for the shorter proopiomelanocortin (POMC) products, such as the alpha-, beta-, and gamma-melanocyte-stimulating hormone (MSH), has appeared later,…

Melanocyte-stimulating hormonePhysiologyMolecular Sequence DataBiochemistryConserved sequenceEvolution MolecularCellular and Molecular NeuroscienceEndocrinologyProopiomelanocortinMelanocortin receptorbiology.animalAnimalsHumansAmino Acid SequenceReceptorConserved SequenceG protein-coupled receptorGeneticsbiologyReceptors MelanocortinVertebrateGenomicsStructural Homology Proteinbiology.proteinMelanocortinhormones hormone substitutes and hormone antagonistsPeptides
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News from an Ancient World: Two Novel Astacin Metalloproteases from the Horseshoe Crab

2008

In this work, we report the cloning, heterologous expression, and characterization of two novel astacin proteases from the chelicerate Limulus polyphemus (horseshoe crab), designated as LAST (Limulus astacin) and LAST_MAM (Limulus astacin containing a MAM domain), respectively. The expression pattern showed ubiquitous occurrence of LAST_MAM, while LAST was predominantly restricted to the eyes and brain, indicating a function in the nervous system. Both enzymes contain the characteristic metzincin-type zinc-binding region and Met turn. While LAST is made up only of the typical prodomain and astacin-like protease domain, LAST_MAM contains an additional MAM (meprin A5 protein tyrosine phosphat…

Models MolecularProteasesDNA ComplementaryInsectaProtein familymedicine.medical_treatmentMolecular Sequence DataContext (language use)Protein tyrosine phosphataseBiologyHydroxamic AcidsNervous SystemCollagen Type IGene Expression Regulation EnzymologicCell LineEvolution MolecularStructural BiologyHorseshoe CrabsmedicineAnimalsProtein oligomerizationAmino Acid SequenceRNA MessengerCloning MolecularMolecular BiologyPhylogenyExtracellular Matrix ProteinsProteaseBase SequenceCaseinsMetalloendopeptidasesbiology.organism_classificationProtein Structure TertiaryBiochemistryStructural Homology ProteinLimulusAstacinOligopeptidesProtein Processing Post-TranslationalJournal of Molecular Biology
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Homology models of melatonin receptors: challenges and recent advances

2013

Melatonin exerts many of its actions through the activation of two G protein-coupled receptors (GPCRs), named MT1 and MT2. So far, a number of different MT1 and MT2 receptor homology models, built either from the prototypic structure of rhodopsin or from recently solved X-ray structures of druggable GPCRs, have been proposed. These receptor models differ in the binding modes hypothesized for melatonin and melatonergic ligands, with distinct patterns of ligand-receptor interactions and putative bioactive conformations of ligands. The receptor models will be described, and they will be discussed in light of the available information from mutagenesis experiments and ligand-based pharmacophore …

Models MolecularProtein Conformationhomology modelingMolecular Sequence DataDruggabilityReviewComputational biologyLigandsBioinformaticsCatalysisInorganic Chemistrylcsh:ChemistryStructure-Activity Relationshipmelatonin receptorsAnimalsHumansAmino Acid SequenceHomology modelingmelatonin receptors; MT1; MT2; homology modeling; structure-activity relationships; docking; molecular dynamics simulationsPhysical and Theoretical ChemistryReceptorMolecular Biologylcsh:QH301-705.5SpectroscopyMelatoninG protein-coupled receptorBinding SitesSequence Homology Amino AcidbiologyReceptor Melatonin MT2Receptor Melatonin MT1MT1Organic ChemistryMT2structure-activity relationshipsGeneral Medicinemolecular dynamics simulationsComputer Science ApplicationsMelatonergiclcsh:Biology (General)lcsh:QD1-999Structural Homology ProteinDocking (molecular)RhodopsindockingMutagenesis Site-Directedbiology.proteinPharmacophore
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IKK-β inhibitors: An analysis of drug–receptor interaction by using Molecular Docking and Pharmacophore 3D-QSAR approaches

2010

Abstract The IKK kinases family represents a thrilling area of research because of its importance in regulating the activity of NF-kB transcription factors. The discovery of the central role played by IKK-β in the activation of transcription in response to apoptotic or inflammatory stimuli allowed to considerate its modulation as a promising tool for the treatment of chronic inflammation and cancer. To date, several IKK-β inhibitors have been discovered and tested. In this work, an analysis of the interactions between different classes of inhibitors and their biological target was performed, through the application of Molecular Docking and Pharmacophore/3D-QSAR approaches to a set of 141 in…

Models MolecularQuantitative structure–activity relationshipReceptors DrugMolecular Sequence DataQuantitative Structure-Activity RelationshipIκB kinaseComputational biologyPharmacologyBiologyMaterials ChemistryHumansAmino Acid SequenceNF-kBHomology modelingPhysical and Theoretical ChemistryProtein Kinase InhibitorsTranscription factorSpectroscopyIKK-betaIKK-beta inhibitors Molecular Docking Pharmacophore 3D-QSAR approachesBinding SitesPharmacophoreKinaseHomology modelingSettore CHIM/08 - Chimica FarmaceuticaComputer Graphics and Computer-Aided DesignI-kappa B KinaseMolecular DockingStructural Homology ProteinBiological targetDrug receptorPharmacophoreJournal of Molecular Graphics and Modelling
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Factors Dictating the Pseudocatalytic Efficiency of Avidins

2006

The hydrolysis of biotinyl p-nitrophenyl ester (BNP) by a series of avidin derivatives was examined. Surprisingly, a hyperthermostable avidin-related protein (AVR4) was shown to display extraordinary yet puzzling hydrolytic activity. In order to evaluate the molecular determinants that contribute to the reaction, the crystal structure of AVR4 was compared with those of avidin, streptavidin and key mutants of the two proteins in complex with biotinyl p-nitroanilide (BNA), the inert amide analogue of BNP. The structures revealed that a critical lysine residue contributes to the hydrolysis of BNP by avidin but has only a minor contribution to the AVR4-mediated reaction. Indeed, the respective …

Models MolecularStreptavidinNitrogenStereochemistryLysineGene ExpressionPlasma protein bindingCrystallography X-RayCatalysischemistry.chemical_compoundProtein structureNucleophileStructural BiologyAmideMolecular BiologyBinding SitesbiologyChemistryHydrolysisLysinePhenyl EthersAvidinLigand (biochemistry)Recombinant ProteinsProtein Structure TertiaryStructural Homology ProteinMutationbiology.proteinStreptavidinProtein BindingAvidinJournal of Molecular Biology
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Structure of the human filamin A actin-binding domain.

2009

Filamin A (FLNa) is a large dimeric protein that binds to actin filaments via its actin-binding domain (ABD). The crystal structure of this domain was solved at 3.2 A resolution. The domain adopts a closed conformation typical of other ABDs, but also forms a dimer both in crystallization conditions and in solution. The structure shows the localization of the residues mutated in patients with periventricular nodular heterotopia or otopalatodigital syndrome. Structural analysis predicts that mutations in both types of disorder may affect actin binding.

Models Molecularanimal structuresDimerFilaminsmacromolecular substancesFilaminCalponin homology domainCrystallography X-Raychemistry.chemical_compoundContractile ProteinsStructural BiologyFLNAHumansProtein Interaction Domains and MotifsActin-binding proteinProtein Structure QuaternaryActinbiologyMicrofilament ProteinsGeneral MedicineActinschemistryStructural Homology ProteinDomain (ring theory)Mutationbiology.proteinBiophysicsBinding domainProtein BindingActa crystallographica. Section D, Biological crystallography
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Two α subunits and one β subunit of meprin zinc-endopeptidases are differentially expressed in the zebrafish Danio rerio

2007

Abstract Meprins are members of the astacin family of metalloproteases expressed in epithelial tissues, intestinal leukocytes and certain cancer cells. In mammals, there are two homologous subunits, which form complex glycosylated disulfide-bonded homo- and heterooligomers. Both human meprin α and meprin β cleave several basement membrane components, suggesting a role in epithelial differentiation and cell migration. There is also evidence that meprin β is involved in immune defence owing to its capability of activating interleukin-1β and the diminished mobility of intestinal leukocytes in meprin β-knockout mice. Here we show for the first time by reverse transcription PCR, immunoblotting a…

Molecular Sequence DataClinical BiochemistryDanioBiochemistryCatalysisChromosomesConserved sequenceAnimalsHumansAmino Acid SequenceRNA MessengerMolecular BiologyPeptide sequenceZebrafishConserved SequencePhylogenyZebrafishRegulation of gene expressionMessenger RNAbiologyMetalloendopeptidasesbiology.organism_classificationMolecular biologyProtein Structure TertiaryCell biologyProtein SubunitsZincGene Expression RegulationMicroscopy FluorescenceStructural Homology Proteinbiology.proteinAstacinSequence AlignmentATP synthase alpha/beta subunitsbchm
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