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Figure 7 | BMC Molecular Biology

Figure 7

From: A point mutation in the DNA-binding domain of HPV-2 E2 protein increases its DNA-binding capacity and reverses its transcriptional regulatory activity on the viral early promoter

Figure 7

Molecular modeling of HPV-2 E2 dimeric DNA-binding domain (prototype and mutated forms). A: Sequence alignment between HPV-2 E2 DNA-Binding domain and HPV-18's (PDB: 1F9F chain: D). There is only one gap between the alignment. In HPV-2 sequence, the A338V mutation is colored red. The secondary structures are derived using the software DSSP. The arrows represent β-strands, and zigzag lines indicate helices. B: The modeled structures of HPV-2 E2 dimeric DNA-Binding domain. Compared to the crystal structure of HPV-18 E2 DNA-Binding domain (PDB: 1F9F), the two helix regions which bind DNA are confirmed (colored cyan). The right structure is mutant form and the residue 338 (Val) is colored red. The modeled structures show that the residue 338 is located in the region of beta barrel

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BMC Molecular Biology

ISSN: 1471-2199

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