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Structures of the N- and C-terminal domains of MHV-A59 nucleocapsid protein corroborate a conserved RNA-protein binding mechanism in coronavirus
Protein & Cell ; (12): 688-697, 2010.
Artigo em Inglês | WPRIM | ID: wpr-757762
ABSTRACT
Coronaviruses are the causative agent of respiratory and enteric diseases in animals and humans. One example is SARS, which caused a worldwide health threat in 2003. In coronaviruses, the structural protein N (nucleocapsid protein) associates with the viral RNA to form the filamentous nucleocapsid and plays a crucial role in genome replication and transcription. The structure of N-terminal domain of MHV N protein also implicated its specific affinity with transcriptional regulatory sequence (TRS) RNA. Here we report the crystal structures of the two proteolytically resistant N- (NTD) and C-terminal (CTD) domains of the N protein from murine hepatitis virus (MHV). The structure of NTD in two different crystal forms was solved to 1.5 Å. The higher resolution provides more detailed structural information than previous reports, showing that the NTD structure from MHV shares a similar overall and topology structure with that of SARS-CoV and IBV, but varies in its potential surface, which indicates a possible difference in RNA-binding module. The structure of CTD was solved to 2.0-Å resolution and revealed a tightly intertwined dimer. This is consistent with analytical ultracentrifugation experiments, suggesting a dimeric assembly of the N protein. The similarity between the structures of these two domains from SARS-CoV, IBV and MHV corroborates a conserved mechanism of nucleocapsid formation for coronaviruses.
Assuntos
Texto completo: DisponíveL Índice: WPRIM (Pacífico Ocidental) Assunto principal: Fosfoproteínas / Ligação Proteica / Sítios de Ligação / RNA / Dados de Sequência Molecular / Química / Alinhamento de Sequência / Sequência de Aminoácidos / Estrutura Terciária de Proteína / Estrutura Secundária de Proteína Idioma: Inglês Revista: Protein & Cell Ano de publicação: 2010 Tipo de documento: Artigo

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Texto completo: DisponíveL Índice: WPRIM (Pacífico Ocidental) Assunto principal: Fosfoproteínas / Ligação Proteica / Sítios de Ligação / RNA / Dados de Sequência Molecular / Química / Alinhamento de Sequência / Sequência de Aminoácidos / Estrutura Terciária de Proteína / Estrutura Secundária de Proteína Idioma: Inglês Revista: Protein & Cell Ano de publicação: 2010 Tipo de documento: Artigo