Characterization of the papillomavirus alpha(1)E2 peptide unfolded to folded transition upon DNA binding.
Transcriptional regulation depends on sequence-specific binding of regulatory proteins to their responsive elements in viral DNA. The papillomavirus E2 protein binds to DNA through the consensus sequence ACCG-NNNN-CGGT, activating or inhibiting viral replication. Through molecular dynamics simulations we were able to characterize the role of the DNA molecule on E2 binding region (named alpha(1)E2) conformation, acquiring structural insights for previous works suggesting an unfolded to folded transition upon alpha(1)E2 complexation to DNA. Moreover, the results indicate sites to guide the design of alpha(1)E2 synthetic derivatives to inhibit the HPV infection.
Giesel
Guilherme Menegon
GM
Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Av Bento Gonçalves 9500, CP 15005, Porto Alegre 91500-970, RS, Brazil.
Lima
Luís Maurício T R
LM
Faber-Barata
Joana
J
Guimarães
Jorge Almeida
JA
Verli
Hugo
H
D000595:Amino Acid Sequence; D000998:Antiviral Agents / Q000737:chemistry / Q000494:pharmacology; D001483:Base Sequence; D004279:DNA, Viral / Q000737:chemistry*; D015195:Drug Design; D008969:Molecular Sequence Data; D009856:Oncogene Proteins, Viral / Q000037:antagonists & inhibitors / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D000998:Antiviral Agents; D004279:DNA, Viral; D009856:Oncogene Proteins, Viral; D010455:Peptides; C069102:oncogene protein E2, Human papillomavirus type 18