CoDNaS-Q: a database of conformational diversity of the native state of proteins with quaternary structure

dc.contributor.affiliationPontificia Universidad Católica del Perú. Departamento de Ciencias
dc.contributor.authorEscobedo, N.
dc.contributor.authorTunque Cahui, R.R.T.
dc.contributor.authorCaruso, G.
dc.contributor.authorRíos, E.G.
dc.contributor.authorHirsh, L.
dc.contributor.authorMonzon, A.M.
dc.contributor.authorParisi, G.
dc.contributor.authorPalopoli, N.
dc.date.accessioned2026-03-13T16:57:37Z
dc.date.issued2022
dc.description.abstractAbstract Summary A collection of conformers that exist in a dynamical equilibrium defines the native state of a protein. The structural differences between them describe their conformational diversity, a defining characteristic of the protein with an essential role in multiple cellular processes. Since most proteins carry out their functions by assembling into complexes, we have developed CoDNaS-Q, the first online resource to explore conformational diversity in homooligomeric proteins. It features a curated collection of redundant protein structures with known quaternary structure. CoDNaS-Q integrates relevant annotations that allow researchers to identify and explore the extent and possible reasons of conformational diversity in homooligomeric protein complexes. Availability and implementation CoDNaS-Q is freely accessible at http://ufq.unq.edu.ar/codnasq/ or https://codnas-q.bioinformatica.org/home. The data can be retrieved from the website. The source code of the database can be downloaded from https://github.com/SfrRonaldo/codnas-q.
dc.description.sponsorshipFunding: The authors would like to thank Martin Gonzalez Buitrón for his help in designing and reviewing CoDNaS-Q. This work was supported by grants from Universidad Nacional de Quilmes (PUNQ 1309/19), Agencia Nacional de Promoción de la Investigación, el Desarrollo Tecnológico y la Innovación (PICT-2018 3457) and Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET) (PIP-2015-2017 11220150100853CO) from Argentina, and the European Union's Horizon 2020 Research and Innovation Staff Exchange program (grant agreements 778247 and 823886). N.E. is a PhD Fellow and G.P. and N.P. are Researchers from CONICET.
dc.identifier.doihttps://doi.org/10.1093/bioinformatics/btac627
dc.identifier.urihttp://hdl.handle.net/20.500.14657/205622
dc.language.isoeng
dc.publisherOxford University Press
dc.relation.ispartofurn:issn:1367-4803
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.sourceBioinformatics; Vol. 38, Núm. 21 (2022)
dc.subjectProtein quaternary structure
dc.subjectDiversity (politics)
dc.subjectConformational isomerism
dc.subjectProtein structure
dc.subjectComputer science
dc.subjectFunctional diversity
dc.subjectSource code
dc.subjectComputational biology
dc.subjectResource (disambiguation)
dc.subjectDatabase
dc.subjectBiology
dc.subjectChemistry
dc.subjectProgramming language
dc.subjectBiochemistry
dc.subjectMolecule
dc.subject.ocdehttps://purl.org/pe-repo/ocde/ford#1.06.00
dc.titleCoDNaS-Q: a database of conformational diversity of the native state of proteins with quaternary structure
dc.typehttp://purl.org/coar/resource_type/c_6501
dc.type.otherArtículo
dc.type.versionhttps://vocabularies.coar-repositories.org/version_types/c_970fb48d4fbd8a85/

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