Skip to main content
. Author manuscript; available in PMC: 2011 Aug 5.
Published in final edited form as: Adv Virus Res. 2008;72:155–205. doi: 10.1016/S0065-3527(08)00404-1

Figure 5. Structures of Papillomavirus E1 and E2 Protein Domains and Complexes.

Figure 5

A. The transactivation domain (residues 1–201) of the HPV-16 E2 protein from the pdb file 1DTO (Antson et al, 2000). Residues R37 and I73 are shown in green and residue D39 is shown in blue.

B. A dimer of the DNA binding/dimerization domain of BPV-1 E2 bound to DNA (residues 326–410) from the pdb file 2BOP (Hegde et al, 1992). The DNA is shown in gray.

C. The transactivation domain of HPV-18 E2 (residues 1–215; red) in complex with a c-terminal domain of HPV18 E1 (residues 428–631; green) from the pdb file 1TUE (Abbate et al, 2004). E2 residue D43 (equivalent to BPV-1 D39 in panel A) is shown in blue.

D. A dimer of the BPV-1 E1 DNA binding domain (residues 159–303) from the pdb file 1FO8 (Enemark et al, 2000). Residues shown in blue are important for DNA contact.

E. Double hexameric ring structure of the BPV-1 E1 helicase domain (residues 306–577) from the pdb file 2GXA (Enemark and Joshua-Tor, 2006). Each E1 monomer is shown in a different color.