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
in English
| LILACS
| ID: lil-544615
Responsible library:
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.
Full text:
Available
Collection:
International databases
Database:
LILACS
Main subject:
DNA, Viral
/
Oncogene Proteins, Viral
/
DNA-Binding Proteins
Language:
English
Journal:
Mem. Inst. Oswaldo Cruz
Journal subject:
Tropical Medicine
/
Parasitology
Year:
2010
Document type:
Article
Affiliation country:
France
/
Venezuela
Institution/Affiliation country:
Centre National de la Recherche Scientifique/FR
/
Instituto de Estudios Avanzados Carretera Nacional Hoyo de la Puerta/VE