Unique structural features of flaviviruses’ capsid proteins: new insights on structure-function relationship

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Federal do Rio de Janeiro (UFRJ)-
Autor(es): dc.contributorUniversidade Estadual Paulista (Unesp)-
Autor(es): dc.creatorNeves-Martins, Thais C.-
Autor(es): dc.creatorMebus-Antunes, Nathane C.-
Autor(es): dc.creatorCaruso, Icaro P. [UNESP]-
Autor(es): dc.creatorAlmeida, Fabio C.L.-
Autor(es): dc.creatorDa Poian, Andrea T.-
Data de aceite: dc.date.accessioned2022-02-22T00:50:12Z-
Data de disponibilização: dc.date.available2022-02-22T00:50:12Z-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2021-04-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1016/j.coviro.2021.02.005-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/207419-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/207419-
Descrição: dc.descriptionThe Flaviviridae family comprises important human pathogens, including Dengue, Zika, West Nile, Yellow Fever and Japanese Encephalitis viruses. The viral genome, a positive-sense single-stranded RNA, is packaged by a single protein, the capsid protein, which is a small and highly basic protein that form intertwined homodimers in solution. Atomic-resolution structures of four flaviviruses capsid proteins were solved either in solution by nuclear magnetic resonance spectroscopy, or after protein crystallization by X-ray diffraction. Analyses of these structures revealed very particular properties, namely (i) the predominance of quaternary contacts maintaining the structure; (ii) a highly electropositive surface throughout the protein; and (iii) a flexible helix (α1). The goal of this review is to discuss the role of these features in protein structure-function relationship.-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ)-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionInstitute of Medical Biochemistry Leopoldo de Meis (IBqM) Federal University of Rio de Janeiro (UFRJ)-
Descrição: dc.descriptionNational Center for Structural Biology and Bioimaging (CENABIO) Federal University of Rio de Janeiro (UFRJ)-
Descrição: dc.descriptionMultiuser Center for Biomolecular Innovation (CMIB) and Department of Physics Institute of Biosciences Letters and Exact Sciences (IBILCE) São Paulo State University (UNESP)-
Descrição: dc.descriptionMultiuser Center for Biomolecular Innovation (CMIB) and Department of Physics Institute of Biosciences Letters and Exact Sciences (IBILCE) São Paulo State University (UNESP)-
Descrição: dc.descriptionFAPERJ: 202.945/2017-
Descrição: dc.descriptionCNPq: 309028/2017-5-
Descrição: dc.descriptionCNPq: 439306/2018-3-
Formato: dc.format106-112-
Idioma: dc.languageen-
Relação: dc.relationCurrent Opinion in Virology-
???dc.source???: dc.sourceScopus-
Título: dc.titleUnique structural features of flaviviruses’ capsid proteins: new insights on structure-function relationship-
Aparece nas coleções:Repositório Institucional - Unesp

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