Assessing protein stability of the dimeric DNA-binding domain of E2 human papillomavirus 18 with molecular dynamics
Mem. Inst. Oswaldo Cruz
; 105(2): 123-126, Mar. 2010. ilus
Article
em En
| LILACS
| ID: lil-544615
Biblioteca responsável:
BR1.1
ABSTRACT
The objective of this study is to understand the structural flexibility and curvature of the E2 protein of human papillomavirus type 18 using molecular dynamics (6 ns). E2 is required for viral DNA replication and its disruption could be an anti-viral strategy. E2 is a dimer, with each monomer folding into a stable open-faced â-sandwich. We calculated the mobility of the E2 dimer and found that it was asymmetric. These different mobilities of E2 monomers suggest that drugs or vaccines could be targeted to the interface between the two monomers.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
LILACS
Assunto principal:
DNA Viral
/
Proteínas Oncogênicas Virais
/
Proteínas de Ligação a DNA
Idioma:
En
Revista:
Mem. Inst. Oswaldo Cruz
Assunto da revista:
MEDICINA TROPICAL
/
PARASITOLOGIA
Ano de publicação:
2010
Tipo de documento:
Article
País de afiliação:
França
/
Venezuela
País de publicação:
Brasil