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Memórias do Instituto Oswaldo Cruz
Fundação Oswaldo Cruz, Fiocruz
ISSN: 1678-8060
EISSN: 1678-8060
Vol. 105, No. 2, 2010, pp. 123-126
Bioline Code: oc10021
Full paper language: English
Document type: Research Article
Document available free of charge

Memórias do Instituto Oswaldo Cruz, Vol. 105, No. 2, 2010, pp. 123-126

 en Assessing protein stability of the dimeric DNA-binding domain of E2 human papillomavirus 18 with molecular dynamics
Isea, Raúl; Ramírez, José Luis & Hoebeke, Johan


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 β-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.

human papillomavirus, molecular dynamics, DNA-binding domain, HPV-18, protein stability

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