Assessing protein stability of the dimeric DNA-binding domain of E2 human papillomavirus 18 with molecular dynamics.
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 beta-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.
Isea
Raúl
R
Centro de Biociencias, Instituto de Estudios Avanzados Carretera Nacional Hoyo de la Puerta, Baruta 1080, Estado Miranda, Venezuela. risea@idea.gob.ve
Ramírez
José Luis
JL
Hoebeke
Johan
J
D004261:DNA Replication; D004279:DNA, Viral / Q000235:genetics* / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000378:metabolism; D019281:Dimerization; D052161:Human papillomavirus 18 / Q000235:genetics* / Q000378:metabolism; D008958:Models, Molecular; D009856:Oncogene Proteins, Viral / Q000235:genetics* / Q000378:metabolism; D055550:Protein Stability; D014779:Virus Replication
D004279:DNA, Viral; D004268:DNA-Binding Proteins; D009856:Oncogene Proteins, Viral; C076036:oncogene protein E2, Human papillomavirus type 1