Data/hora: 02/06/2024 05:39:55

Provedor de dados: | 58
País: | Brazil
Título: | Structural analysis of human respiratory syncytial virus P protein: identification of intrinsically disordered domains
Autores: | Simabuco,Fernando M; Asara,John M; Guerrero,Manuel C; Libermann,Towia A; Zerbini,Luiz F; Ventura,Armando M.
Data: | 2011-03-01
Ano: | 2011
Palavras-chave: | Human respiratory syncytial virus; P protein; Intrinsically disordered domains; Oligomerization.
Resumo: | Human Respiratory Syncytial Virus P protein plus the viral RNA, N and L viral proteins, constitute the viral replication complex. In this report we describe that HRSV P protein has putative intrinsically disordered domains predicted by in silico methods. These two domains, located at the amino and caboxi terminus, were identified by mass spectrometry analysis of peptides obtained from degradation fragments observed in purified P protein expressed in bacteria. The degradation is not occurring at the central oligomerization domain, since we also demonstrate that the purified fragments are able to oligomerize, similarly to the protein expressed in cells infected by HRSV. Disordered domains can play a role in protein interaction, and the present data contribute to the comprehension of HRSV P protein interactions in the viral replication complex.
Tipo: | Info:eu-repo/semantics/article
Idioma: | Inglês
Identificador: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822011000100043
Editor: | Sociedade Brasileira de Microbiologia
Relação: | 10.1590/S1517-83822011000100043
Formato: | text/html
Fonte: | Brazilian Journal of Microbiology  v.42 n.1 2011
Fonte: | info:eu-repo/semantics/openAccess