Structural determination of importin alpha in complex with beak and feather disease virus capsid nuclear localization signal.
Biochem Biophys Res Commun
; 438(4): 680-5, 2013 Sep 06.
Article
em En
| MEDLINE
| ID: mdl-23933059
ABSTRACT
Circoviruses represent a rapidly increasing genus of viruses that infect a variety of vertebrates. Replication requires shuttling viral molecules into the host cell nucleus, a process facilitated by capsid-associated protein (Cap). Whilst a nuclear localization signal (NLS) has been shown to mediate nuclear translocation, the mode of nuclear transport remains to be elucidated. To better understand this process, beak and feather disease virus (BFDV) Cap NLS was crystallized with nuclear import receptor importin-α (Impα). Diffraction yielded structural data to 2.9Å resolution, and the binding site on both Impα and BFDV Cap NLS were well resolved. The binding mechanism for the major site is likely conserved across circoviruses as supported by the similarity of NLSs in circovirus Caps. This finding illuminates a crucial step for infection of host cells by this viral family, and provides a platform for rational drug design against the binding interface.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Circovirus
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Infecções por Circoviridae
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Sinais de Localização Nuclear
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Alfa Carioferinas
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Proteínas do Capsídeo
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Interações Hospedeiro-Patógeno
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article