ArticleNucleic acids research2006
The recognition of local DNA conformation by the human papillomavirus type 6 E2 protein.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Structural and functional roles of conserved residues of human papillomavirus (HPV) E2 protein and biological consequences.Virology journal · 2025Article
- Lymphocyte subsets predictive value and possible involvement of human papilloma virus infection on breast cancer molecular subtypes.World journal of clinical oncology · 2018Article
- Presence of human papillomavirus in breast cancer and its association with prognostic factors.Ecancermedicalscience · 2015Article
- The papillomavirus E2 proteins.Virology · 2013Review
- Protein flexibility directs DNA recognition by the papillomavirus E2 proteins.Nucleic acids research · 2011Article
- Thermodynamics of cooperative DNA recognition at a replication origin and transcription regulatory site.Biochemistry · 2010Article
- Experimental snapshots of a protein-DNA binding landscape.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Human papillomavirus (HPV) type 18 induces extended growth in primary human cervical, tonsillar, or foreskin keratinocytes more effectively than other high-risk mucosal HPVs.Journal of virology · 2009Article
- Transition state for protein-DNA recognition.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Comprehensive comparison of the interaction of the E2 master regulator with its cognate target DNA sites in 73 human papillomavirus types by sequence statistics.Nucleic acids research · 2008Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The E2 proteins are transcription/replication factors from papillomaviruses. Human papillomaviruses (HPVs) can be broadly divided in two groups; low-risk HPV subtypes cause benign warts while high-risk HPVs give rise to cervical cancer. Although a range of crystal structures of E2 DNA-binding domains (DBD) from both high- and low-risk HPV subtypes have been reported previously, structures of E2 DBD:DNA complexes have only been available for high-risk HPV18 and bovine papillomavirus (BPV1). In the present study we report the unliganded and DNA complex structures of the E2 DBD from the low-risk HPV6. As in the previous E2-DNA structures, complex formation results in considerable bending of the DNA, which is facilitated by sequences with A:T-rich spacers that adopt a pre-bent conformation. The low-risk HPV6 E2-DNA complex differs from the earlier structures in that minimal deformation of the protein accompanies complex formation. Stopped-flow kinetic studies confirm that both high- and low-risk E2 proteins adapt their structures on binding to DNA, although this is achieved more readily for HPV6 E2. It therefore appears that the higher selectivity of the HPV6 E2 protein may arise from its limited molecular adaptability, a property that might distinguish the behaviour of E2 proteins from high- and low-risk HPV subtypes.
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