Search results for "Protein Data Bank"

showing 10 items of 23 documents

Evaluating protein structures determined by structural genomics consortia.

2006

Structural genomics projects are providing large quantities of new 3D structural data for proteins. To monitor the quality of these data, we have developed the protein structure validation software suite (PSVS), for assessment of protein structures generated by NMR or X-ray crystallographic methods. PSVS is broadly applicable for structure quality assessment in structural biology projects. The software integrates under a single interface analyses from several widely-used structure quality evaluation tools, including PROCHECK (Laskowski et al., J Appl Crystallog 1993;26:283-291), MolProbity (Lovell et al., Proteins 2003;50:437-450), Verify3D (Luthy et al., Nature 1992;356:83-85), ProsaII (Si…

Models MolecularComputer scienceProtein Data Bank (RCSB PDB)GenomicsComputational biologycomputer.software_genreCrystallography X-RayBiochemistryStructural genomicsProtein structureStructural BiologySoftware DesignHumansDatabases ProteinMolecular BiologyNuclear Magnetic Resonance BiomolecularSoftware suiteComputational BiologyProteinsGenomicsProtein Structure TertiaryCrystallographyStructural biologyQuality ScorecomputerData integrationProteins
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Evolution of molluscan hemocyanin structures

2013

AbstractHemocyanin transports oxygen in the hemolymph of many molluscs and arthropods and is therefore a central physiological factor in these animals. Molluscan hemocyanin molecules are oligomers composed of many protein subunits that in turn encompass subsets of distinct functional units. The structure and evolution of molluscan hemocyanin have been studied for decades, but it required the recent progress in DNA sequencing, X-ray crystallography and 3D electron microscopy to produce a detailed view of their structure and evolution. The basic quaternary structure is a cylindrical decamer 35nm in diameter, consisting of wall and collar (typically at one end of the cylinder). Depending on th…

Models MolecularEvolutionProtein Conformationmedicine.medical_treatmentProtein subunitProtein Data Bank (RCSB PDB)BiophysicsCrystallography X-RayHemocyaninBiochemistryAnalytical ChemistryRespiratory proteinsPaleontologyHemolymphElectron microscopymedicineQuaternary structureAnimalsMolecular BiologybiologyHemocyanincomputer.file_formatKeyhole limpet hemocyaninProtein Data BankBiological EvolutionMolluscaEvolutionary biologyHemocyaninsbiology.proteinProtein quaternary structureKLHcomputerKeyhole limpet hemocyaninOxygen bindingBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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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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Quality assessment of protein NMR structures.

2013

Biomolecular NMR structures are now routinely used in biology, chemistry, and bioinformatics. Methods and metrics for assessing the accuracy and precision of protein NMR structures are beginning to be standardized across the biological NMR community. These include both knowledge-based assessment metrics, parameterized from the database of protein structures, and model versus data assessment metrics. On line servers are available that provide comprehensive protein structure quality assessment reports, and efforts are in progress by the world-wide Protein Data Bank (wwPDB) to develop a biomolecular NMR structure quality assessment pipeline as part of the structure deposition process. These qu…

Models MolecularProtein structure; NMR spectroscopyMagnetic Resonance SpectroscopyProtein ConformationAnalytical chemistryBiology010402 general chemistrycomputer.software_genre01 natural sciencesArticle03 medical and health sciencesStructural BiologyServerDatabases ProteinMolecular BiologyNuclear Magnetic Resonance Biomolecular030304 developmental biology0303 health sciencesExtramuralQuality assessmentData assessmentResearchProteinsReproducibility of ResultsNuclear magnetic resonance spectroscopycomputer.file_formatProtein Data Bank0104 chemical sciencesData miningcomputerDeposition processCurrent opinion in structural biology
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Structure-based analyses of Salmonella RcsB variants unravel new features of the Rcs regulon

2021

18 páginas, 7 figuras, 2 tablas

Models MolecularSalmonella typhimuriumIdentificationSignaling SystemTranscription GeneticTranscription FactorAcademicSubjects/SCI00010Protein ConformationProtein Data Bank (RCSB PDB)ExpressionBiologymedicine.disease_causeRegulonBiofilm Formation03 medical and health sciencesBacterial ProteinsCapsule SynthesisStructural BiologyGeneticsmedicineTranscriptional regulationPhosphorylationPromoter Regions GeneticTranscription factorGene030304 developmental biologyRegulation of gene expression0303 health sciencesMutationBinding Sites030306 microbiologyPromoterGene Expression Regulation BacterialBiología y Biomedicina / BiologíaRepressionCell biologyRegulonEscherichia-Coli K-12MutationGenome BacterialPhosphorelay SystemNucleic Acids Research
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Protein knot server: detection of knots in protein structures

2007

KNOTS (http://knots.mit.edu) is a web server that detects knots in protein structures. Several protein structures have been reported to contain intricate knots. The physiological role of knots and their effect on folding and evolution is an area of active research. The user submits a PDB id or uploads a 3D protein structure in PDB or mmCIF format. The current implementation of the server uses the Alexander polynomial to detect knots. The results of the analysis that are presented to the user are the location of the knot in the structure, the type of the knot and an interactive visualization of the knot. The results can also be downloaded and viewed offline. The server also maintains a regul…

Models MolecularWeb serverProtein FoldingTheoretical computer scienceProtein ConformationProtein Data Bank (RCSB PDB)MathematicsofComputing_NUMERICALANALYSISAlexander polynomialBiologyBioinformaticscomputer.software_genreUploadUser-Computer InterfaceKnot (unit)Protein structureTheoryofComputation_ANALYSISOFALGORITHMSANDPROBLEMCOMPLEXITYComputingMethodologies_SYMBOLICANDALGEBRAICMANIPULATIONGeneticsComputer SimulationSurgical knotsDatabases ProteinInteractive visualizationComputingMethodologies_COMPUTERGRAPHICSInternetQuantitative Biology::BiomoleculesModels StatisticalComputational BiologyProteinsArticlesHaemophilus influenzaeMathematics::Geometric TopologycomputerAlgorithmsSoftwareMathematicsofComputing_DISCRETEMATHEMATICS
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MCC1019, a selective inhibitor of the Polo-box domain of Polo-like kinase 1 as novel, potent anticancer candidate

2019

Polo-like kinase (PLK1) has been identified as a potential target for cancer treatment. Although a number of small molecules have been investigated as PLK1 inhibitors, many of which showed limited selectivity. PLK1 harbors a regulatory domain, the Polo box domain (PBD), which has a key regulatory function for kinase activity and substrate recognition. We report on 3-bromomethyl-benzofuran-2-carboxylic acid ethyl ester (designated: MCC1019) as selective PLK1 inhibitor targeting PLK1 PBD. Cytotoxicity and fluorescence polarization-based screening were applied to a library of 1162 drug-like compounds to identify potential inhibitors of PLK1 PBD. The activity of compound MC1019 against the PLK1…

PBD Polo box domainMTD maximal tolerance doseCDC25 cell division cycle 25HIF-1α hypoxia-inducible factor 1 αMST microscale thermophoresisIC50 50% inhibition concentrationMFP M phase promoting factorPARP-1 poly(ADP-ribose) polymerase-10302 clinical medicineFOXO forkhead box ONec-1 necrostatin 1CDC2 cell division cycle protein 2 homologGeneral Pharmacology Toxicology and PharmaceuticsMitotic catastropheCDK cyclin-dependent kinase0303 health sciencesChemistryPolo-like kinaseMono-targeted therapyCell cycleBUBR1 budding uninhibited by benzimidazole-related 1Polo box domain030220 oncology & carcinogenesisPLK1 Polo-like kinaseNecroptosisSpindle damagePLK1IHC immunohistochemistryOriginal articleNecroptosisCell cyclePLK1APC/C anaphase-promoting complex/cyclosomePLK3ABC avidin-biotin complexPI propidium iodide03 medical and health sciencesFBS fetal bovine serumPDB Protein Data BankKd the dissociation constantKinase activity030304 developmental biologyAkt/PKB signaling pathwayCell growthlcsh:RM1-950LC3 light chain 3lcsh:Therapeutics. PharmacologyCancer researchDAPKs death-associated protein kinase3-MA 3-methyladenineDAPI 4′6-diamidino-2-phenylindoleSAC spindle assembly checkpointActa Pharmaceutica Sinica B
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A Stevedore's protein knot.

2009

Protein knots, mostly regarded as intriguing oddities, are gradually being recognized as significant structural motifs. Seven distinctly knotted folds have already been identified. It is by and large unclear how these exceptional structures actually fold, and only recently, experiments and simulations have begun to shed some light on this issue. In checking the new protein structures submitted to the Protein Data Bank, we encountered the most complex and the smallest knots to date: A recently uncovered α-haloacid dehalogenase structure contains a knot with six crossings, a so-called Stevedore knot, in a projection onto a plane. The smallest protein knot is present in an as yet unclassified …

Protein FoldingHydrolasesProtein ConformationComputational Biology/Macromolecular Structure Analysis02 engineering and technologyBiologyMolecular Dynamics SimulationComputational Biology/Molecular DynamicsCombinatorics03 medical and health sciencesCellular and Molecular NeuroscienceKnot (unit)Protein structureGeneticsStructural motifDatabases ProteinMolecular Biologylcsh:QH301-705.5Ecology Evolution Behavior and Systematics030304 developmental biology0303 health sciencesTopological complexityQuantitative Biology::BiomoleculesEcologycomputer.file_format021001 nanoscience & nanotechnologyProtein Data BankMathematics::Geometric TopologyComputational Theory and MathematicsBiochemistrylcsh:Biology (General)Modeling and SimulationProtein foldingStevedore knot0210 nano-technologySingle loopcomputerResearch ArticlePLoS Computational Biology
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Proteins' Knotty Problems

2018

Abstract Knots in proteins are increasingly being recognized as an important structural concept, and the folding of these peculiar structures still poses considerable challenges. From a functional point of view, most protein knots discovered so far are either enzymes or DNA-binding proteins. Our comprehensive topological analysis of the Protein Data Bank reveals several novel structures including knotted mitochondrial proteins and the most deeply embedded protein knot discovered so far. For the latter, we propose a novel folding pathway based on the idea that a loose knot forms at a terminus and slides to its native position. For the mitochondrial proteins, we discuss the folding problem fr…

Protein FoldingProtein ConformationComputational biologyMitochondrial Proteins03 medical and health sciences0302 clinical medicineKnot (unit)Protein structurestomatognathic systemStructural BiologyHumansDatabases ProteinMolecular BiologyMitochondrial protein030304 developmental biologyPhysics0303 health sciencesMembrane Proteinsfood and beveragescomputer.file_formatProtein Data BankMitochondriaDNA-Binding Proteinssurgical procedures operativeMembrane proteincomputer030217 neurology & neurosurgeryJournal of Molecular Biology
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A computer system to perform structure comparison using TOPS representations of protein structure

2001

We describe the design and implementation of a fast topology-based method for protein structure comparison. The approach uses the TOPS topological representation of protein structure, aligning two structures using a common discovered pattern and generating measure of distance derived from an insert score. Heavy use is made of a constraint-based pattern-matching algorithm for TOPS diagrams that we have designed and described elsewhere (Bioinformatics 15(4) (1999) 317). The comparison system is maintained at the European Bioinformatics Institute and is available over the Web at tops.ebi.ac.uk/tops. Users submit a structure description in Protein Data Bank (PDB) format and can compare it with …

Protein structure databaseMeasure (data warehouse)Molecular StructureComputer scienceGeneral Chemical EngineeringProteinsSequence Homologycomputer.file_formatTOPSProtein structure predictioncomputer.software_genreProtein Data BankApplied Microbiology and BiotechnologyPattern Recognition AutomatedArtificial IntelligencePattern matchingData miningProtein topologyRepresentation (mathematics)computerAlgorithmsSoftwareBiotechnology
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