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
Artículo
en Inglés
| LILACS
| ID: lil-544615
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.
Texto completo:
Disponible
Índice:
LILACS (Américas)
Asunto principal:
ADN Viral
/
Proteínas Oncogénicas Virales
/
Proteínas de Unión al ADN
Idioma:
Inglés
Revista:
Mem. Inst. Oswaldo Cruz
Asunto de la revista:
Medicina Tropical
/
Parasitología
Año:
2010
Tipo del documento:
Artículo
País de afiliación:
Francia
/
Venezuela
Institución/País de afiliación:
Centre National de la Recherche Scientifique/FR
/
Instituto de Estudios Avanzados Carretera Nacional Hoyo de la Puerta/VE
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