Search results for " Homology"

showing 10 items of 633 documents

Homology modeling using simulated annealing of restrained molecular dynamics and conformational search calculations with CONGEN: application in predi…

1997

We have developed an automatic approach for homology modeling using restrained molecular dynamics and simulated annealing procedures, together with conformational search algorithms available in the molecular mechanics program CONGEN (Bruccoleri RE, Karplus M, 1987, Biopolymers 26:137-168). The accuracy of the method is validated by "predicting" structures of two homeodomain proteins with known three-dimensional structures, and then applied to predict the three-dimensional structure of the homeodomain of the murine Msx-1 transcription factor. Regions of the unknown protein structure that are highly homologous to the known template structure are constrained by "homology distance constraints,"…

Models MolecularSaccharomyces cerevisiae ProteinsProtein ConformationMSX1 Transcription FactorMolecular Sequence DataSaccharomyces cerevisiaeBiologyProtein EngineeringBiochemistryProtein Structure SecondaryMolecular dynamicsMiceProtein structureAnimalsComputer SimulationHomology modelingAmino Acid SequenceMolecular BiologyHomeodomain ProteinsMSX1 Transcription FactorSequence Homology Amino AcidNuclear ProteinsProtein engineeringProtein superfamilyengrailedRepressor ProteinsCrystallographyAntennapedia Homeodomain ProteinThreading (protein sequence)AlgorithmsInformation SystemsTranscription FactorsResearch ArticleProtein science : a publication of the Protein Society
researchProduct

Molecular modelling study of the role of cholesterol in the stimulation of the oxytocin receptor.

2001

Cholesterol, an integral component of membranes in Eucaryota, is a modifier of membrane properties. In vivo studies have demonstrated that cholesterol can also modulate activities of some G protein-coupled receptors (GPCRs), which are integral membrane proteins. This can result either from an effect of cholesterol on the membrane fluidity or from specific interactions of the membrane cholesterol with the receptor, as recently demonstrated for the cholecystokinin type beta (CCKRbeta) or the oxytocin receptor (OTR). Using molecular modelling, we studied conformational preferences of cholesterol and several of its analogues. Subsequently, we simulated the distributions of their preferred confo…

Models MolecularSequence Homology Amino AcidProtein ConformationMolecular Sequence DataBiologyCholecystokinin receptorOxytocin receptorGeneral Biochemistry Genetics and Molecular BiologySterolSterolsCholesterolBiochemistryReceptors OxytocinMutationBiophysicsMembrane fluidityHumansAmino Acid SequenceReceptorCholecystokininIntegral membrane proteinhormones hormone substitutes and hormone antagonistsCholecystokininG protein-coupled receptorProtein BindingActa biochimica Polonica
researchProduct

The Sequence of a Gastropod Hemocyanin (HtH1 from Haliotis tuberculata)

2000

The eight functional units (FUs), a-h, of the hemocyanin isoform HtH1 from Haliotis tuberculata (Prosobranchia, Archaeogastropoda) have been sequenced via cDNA, which provides the first complete primary structure of a gastropod hemocyanin subunit. With 3404 amino acids (392 kDa) it is the largest polypeptide sequence ever obtained for a respiratory protein. The cDNA comprises 10,758 base pairs and includes the coding regions for a short signal peptide, the eight different functional units, a 3'-untranslated region of 478 base pairs, and a poly(A) tail. The predicted protein contains 13 potential sites for N-linked carbohydrates (one for HtH1-a, none for HtH1-c, and two each for the other si…

Models MolecularSignal peptideDNA ComplementaryProtein subunitmedicine.medical_treatmentMolecular Sequence DataOctopodiformesBiologyBiochemistryEvolution MolecularArchaeogastropodaComplementary DNAmedicineAnimalsProtein IsoformsComputer SimulationAmino Acid SequenceMolecular BiologyPeptide sequencePhylogenyGene LibrarySequence Homology Amino AcidProtein primary structureHemocyaninCell BiologyAnatomybiology.organism_classificationRespiratory proteinBiochemistryMolluscaHemocyaninsProtein BindingJournal of Biological Chemistry
researchProduct

The 1.45 A resolution structure of the cryptogein-cholesterol complex: a close-up view of a sterol carrier protein (SCP) active site.

2002

Cryptogein is a small 10 kDa elicitor produced by the phytoparasitic oomycete Phytophthora cryptogea. The protein also displays a sterol carrier activity. The native protein crystallizes in space group P4(1)22, with unit-cell parameters a = b = 46.51, c = 134.9 A (diffraction limit: 2.1 A). Its complex with cholesterol crystallizes in space group C222(1), with unit-cell parameters a = 30.96, b = 94.8, c = 65.3 A and a resolution enhanced to 1.45 A. The large inner non-specific hydrophobic cavity is able to accommodate a large variety of 3-beta-hydroxy sterols. Cryptogein probably acts as a sterol shuttle helping the pathogen to grow and complete its life cycle.

Models MolecularStereochemistryMolecular Sequence DataBiologyFungal Proteinschemistry.chemical_compoundStructural BiologyAmino Acid SequenceOomyceteBinding SitesMolecular StructureSequence Homology Amino AcidCholesterolPhytophthora cryptogeaResolution (electron density)Algal ProteinsActive siteGeneral Medicinebiology.organism_classificationSterolElicitorSterolsSterol carrier proteinCholesterolBiochemistrychemistrybiology.proteinCarrier ProteinsActa crystallographica. Section D, Biological crystallography
researchProduct

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
researchProduct

Structural insights into the GTPase domain of Escherichia coli MnmE protein

2007

The Escherichia coli MnmE protein is a 50-kDa multidomain GTPase involved in tRNA modification. Its homologues in eukaryotes are crucial for mitochondrial respiration and, thus, it is thought that the human protein might be involved in mitochondrial diseases. Unlike Ras, MnmE shows a high intrinsic GTPase activity and requires effective GTP hydrolysis, and not simply GTP binding, to be functionally active. The isolated MnmE G-domain (165 residues) conserves the GTPase activity of the entire protein, suggesting that it contains the catalytic residues for GTP hydrolysis. To explore the GTP hydrolysis mechanism of MnmE, we analyzed the effect of low pH on binding and hydrolysis of GTP, as well…

Models MolecularTRNA modificationMagnetic Resonance SpectroscopyGTP'aluminium fluoridehomology modelingMolecular Sequence DataGTPaseGuanosine triphosphateGuanosine DiphosphateBiochemistryeraGTP Phosphohydrolaseschemistry.chemical_compoundStructural BiologyEscherichia coliAmino Acid SequenceHomology modelingBinding siteGTPaseMolecular BiologyBinding SitesSequence Homology Amino AcidChemistryEscherichia coli ProteinsTrmENMRRecombinant ProteinsKineticsBiochemistryMnmEGuanosine diphosphateRap2AGTP PhosphohydrolasesGuanosine TriphosphateSequence AlignmentRasProteins: Structure, Function, and Bioinformatics
researchProduct

The molecular basis of filamin binding to integrins and competition with talin.

2006

The ability of adhesion receptors to transmit biochemical signals and mechanical force across cell membranes depends on interactions with the actin cytoskeleton. Filamins are large, actin-crosslinking proteins that connect multiple transmembrane and signaling proteins to the cytoskeleton. Here, we describe the high-resolution structure of an interface between filamin A and an integrin adhesion receptor. When bound, the integrin beta cytoplasmic tail forms an extended beta strand that interacts with beta strands C and D of the filamin immunoglobulin-like domain (IgFLN) 21. This interface is common to many integrins, and we suggest it is a prototype for other IgFLN domain interactions. Notabl…

Models MolecularTalinanimal structuresIntegrin beta ChainsProtein ConformationFilaminsRecombinant Fusion ProteinsIntegrinMolecular Sequence Datamacromolecular substancesPlasma protein bindingFilaminCrystallography X-RayFilamin bindingMiceContractile ProteinsFLNAAnimalsAmino Acid SequenceMolecular BiologyNuclear Magnetic Resonance BiomolecularBinding SitesbiologySequence Homology Amino AcidCalpainMicrofilament ProteinsReproducibility of ResultsCell BiologyActin cytoskeletonCell biologyProtein Structure Tertiarybody regionsIntegrin alpha Mbiology.proteinNIH 3T3 CellsIntegrin beta 6Protein BindingMolecular cell
researchProduct

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
researchProduct

Characterization of aCandida albicansgene encoding a putative transcriptional factor required for cell wall integrity

2003

After screening a Candida albicans genome database the product of an open reading frame (ORF) (CA2880) with 49% homology to the product of Saccharomyces cerevisiae YPL133c, a putative transcriptional factor, was identified. The disruption of the C. albicans gene leads to a major sensitivity to calcofluor white and Congo red, a minor sensitivity to sodium dodecyl sulfate, a major resistance to zymolyase, and an alteration of the chemical composition of the cell wall. For these reasons we called it CaCWT1 (for C. albicans cell wall transcription factor). CaCwt1p contains a putative Zn(II) Cys(6) DNA binding domain characteristic of some transcriptional factors and a PAS domain. The CaCWT1 gen…

Models MolecularTranscription GeneticGenes FungalMolecular Sequence DataSaccharomyces cerevisiaeSequence HomologyMicrobiologyFungal ProteinsCell WallPAS domainGene Expression Regulation FungalCandida albicansGenes RegulatorGeneticsAmino Acid SequenceColoring AgentsCandida albicansMolecular BiologyGeneTranscription factorbiologyReverse Transcriptase Polymerase Chain ReactionGlucan Endo-13-beta-D-GlucosidaseComputational BiologySodium Dodecyl SulfateDNA-binding domainbiology.organism_classificationMolecular biologyCorpus albicansDNA-Binding ProteinsMutagenesis InsertionalOpen reading frameGenome FungalGene DeletionTranscription FactorsFEMS Microbiology Letters
researchProduct

The Structure of Rauvolfia serpentina Strictosidine Synthase Is a Novel Six-Bladed β-Propeller Fold in Plant Proteins

2006

Abstract The enzyme strictosidine synthase (STR1) from the Indian medicinal plant Rauvolfia serpentina is of primary importance for the biosynthetic pathway of the indole alkaloid ajmaline. Moreover, STR1 initiates all biosynthetic pathways leading to the entire monoterpenoid indole alkaloid family representing an enormous structural variety of ∼2000 compounds in higher plants. The crystal structures of STR1 in complex with its natural substrates tryptamine and secologanin provide structural understanding of the observed substrate preference and identify residues lining the active site surface that contact the substrates. STR1 catalyzes a Pictet-Spengler–type reaction and represents a novel…

Models MolecularTryptamineProtein FoldingStrictosidine synthaseProtein ConformationMolecular Sequence DataSequence alignmentPlant ScienceCatalysisRauwolfiaSubstrate Specificitychemistry.chemical_compoundRauvolfia serpentinaCarbon-Nitrogen LyasesAmino Acid SequenceResearch ArticlesConserved SequencePlant ProteinsBinding SitesSequence Homology Amino AcidbiologyIndole alkaloidActive siteCell BiologyLyasebiology.organism_classificationTryptamineschemistryBiochemistrybiology.proteinSecologaninSequence AlignmentThe Plant Cell
researchProduct