dc.contributor | Universidade Federal do Rio de Janeiro (UFRJ) | |
dc.contributor | Universidade Estadual Paulista (Unesp) | |
dc.date.accessioned | 2021-06-25T10:54:53Z | |
dc.date.accessioned | 2022-12-19T22:28:50Z | |
dc.date.available | 2021-06-25T10:54:53Z | |
dc.date.available | 2022-12-19T22:28:50Z | |
dc.date.created | 2021-06-25T10:54:53Z | |
dc.date.issued | 2021-04-01 | |
dc.identifier | Current Opinion in Virology, v. 47, p. 106-112. | |
dc.identifier | 1879-6265 | |
dc.identifier | 1879-6257 | |
dc.identifier | http://hdl.handle.net/11449/207419 | |
dc.identifier | 10.1016/j.coviro.2021.02.005 | |
dc.identifier | 2-s2.0-85102256124 | |
dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/5388016 | |
dc.description.abstract | The 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. | |
dc.language | eng | |
dc.relation | Current Opinion in Virology | |
dc.source | Scopus | |
dc.title | Unique structural features of flaviviruses’ capsid proteins: new insights on structure-function relationship | |
dc.type | Otros | |