Search results for "Data bank"

showing 5 items of 25 documents

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
researchProduct

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
researchProduct

Prospective computational design and in vitro bio-analytical tests of new chemical entities as potential selective CYP17A1 lyase inhibitors

2019

[EN] The development and advancement of prostate cancer (PCa) into stage 4, where it metastasize, is a major problem mostly in elder males. The growth of PCa cells is stirred up by androgens and androgen receptor (AR). Therefore, therapeutic strategies such as blocking androgens synthesis and inhibiting AR binding have been explored in recent years. However, recently approved drugs (or in clinical phase) failed in improving the expected survival rates for this metastatic-castration resistant prostate cancer (mCRPC) patients. The selective CYP17A1 inhibition of 17,20-lyase route has emerged as a novel strategy. Such inhibition blocks the production of androgens everywhere they are found in t…

Quantitative structure–activity relationshipStereochemistry01 natural sciencesBiochemistryStructure-Activity Relationship3D-QSAR pharmacophore modelDrug DiscoveryCytochrome P-450 Enzyme InhibitorsHumansStructure–activity relationshipCYP17A1 InhibitorMolecular BiologyDensity Functional TheoryVirtual screeningDose-Response Relationship DrugMolecular Structure010405 organic chemistryChemistryOrganic ChemistryProspective computational designSteroid 17-alpha-Hydroxylasecomputer.file_format1720-lyase selective inhibitionProtein Data BankLyase0104 chemical sciencesMolecular Docking Simulation010404 medicinal & biomolecular chemistryDocking (molecular)CYP17A1 inhibitorsMetastatic-castration resistant prostate cancerPharmacophorecomputer
researchProduct

RepeatsDB in 2021: improved data and extended classification for protein tandem repeat structures

2020

The RepeatsDB database (URL: https://repeatsdb.org/) provides annotations and classification for protein tandem repeat structures from the Protein Data Bank (PDB). Protein tandem repeats are ubiquitous in all branches of the tree of life. The accumulation of solved repeat structures provides new possibilities for classification and detection, but also increasing the need for annotation. Here we present RepeatsDB 3.0, which addresses these challenges and presents an extended classification scheme. The major conceptual change compared to the previous version is the hierarchical classification combining top levels based solely on structural similarity (Class > Topology > Fold) with two new lev…

Repetitive Sequences Amino AcidAcademicSubjects/SCI00010BiologíaStatistics as TopicProtein Data Bank (RCSB PDB)Computational biologyBiologyRepetitive SequencesGene Ontology; HEK293 Cells; HeLa Cells; Humans; Proteins; Reproducibility of Results; Statistics as Topic; User-Computer Interface; Databases Protein; Repetitive Sequences Amino Acid; Tandem Repeat SequencesDatabases03 medical and health sciencesAnnotationUser-Computer InterfaceProtein structureSimilarity (network science)Tandem repeatGeneticsDatabase IssueHumansDatabases ProteinCiencias Exactasdatabase030304 developmental biology0303 health sciencesHierarchy (mathematics)Protein030302 biochemistry & molecular biologyProteinsReproducibility of Resultscomputer.file_formatProtein Data BankClass (biology)proteinsAmino AcidComputingMethodologies_PATTERNRECOGNITIONGene OntologyHEK293 CellsclassificationTandem Repeat Sequencesprotein tandem repeat structures[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]computerHeLa CellsNucleic Acids Research
researchProduct

Local vs global motions in protein folding

2013

It is of interest to know whether local fluctuations in a polypeptide chain play any role in the mechanism by which the chain folds to the native structure of a protein. This question is addressed by analyzing folding and non-folding trajectories of a protein; as an example, the analysis is applied to the 37-residue triple β-strand WW domain from the Formin binding protein 28 (FBP28) (PDB ID: 1E0L). Molecular dynamics (MD) trajectories were generated with the coarse-grained united-residue force field, and one- and two-dimensional free-energy landscapes (FELs) along the backbone virtual-bond angle θ and backbone virtual-bond-dihedral angle γ of each residue, and principal components, respect…

biologyChemistryBinding proteinProtein Data Bank (RCSB PDB)NanotechnologyForce field (chemistry)ArticleComputer Science ApplicationsWW domainMolecular dynamicsForminsPrincipal component analysisbiology.proteinProtein foldingPhysical and Theoretical ChemistryBiological system
researchProduct