1F9F

CRYSTAL STRUCTURE OF THE HPV-18 E2 DNA-BINDING DOMAIN

1F9F の概要

• エントリーDOI: 10.2210/pdb1f9f/pdb
• 分子名称: Regulatory protein E2, SULFATE ION (3 entities in total)
• 機能のキーワード: dimeric beta barrel, activator, dna-binding, trans-acting factor, transcription
• 由来する生物種: Human papillomavirus type 18
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 38548.03

構造登録者

Kim, S.S.,Tam, J.,Wang, A.F.,Hegde, R. (登録日: 2000-07-10, 公開日: 2000-11-15, 最終更新日: 2024-02-07)

主引用文献

Kim, S.S.,Tam, J.K.,Wang, A.F.,Hegde, R.S.
The structural basis of DNA target discrimination by papillomavirus E2 proteins.
J.Biol.Chem., 275:31245-31254, 2000

PubMed Abstract: The papillomavirus E2 proteins regulate the transcription of all papillomavirus genes and are necessary for viral DNA replication. Disruption of the E2 gene is commonly associated with malignancy in cervical carcinoma, indicating that E2 has a role in regulating tumor progression. Although the E2 proteins from all characterized papillomaviruses bind specifically to the same 12-base pair DNA sequence, the cancer-associated human papillomavirus E2 proteins display a unique ability to detect DNA flexibility and intrinsic curvature. To understand the structural basis for this phenomenon, we have determined the crystal structures of the human papillomavirus-18 E2 DNA-binding domain and its complexes with high and low affinity binding sites. The E2 protein is a dimeric beta-barrel and the E2-DNA interaction is accompanied by a large deformation of the DNA as it conforms to the E2 surface. DNA conformation and E2-DNA contacts are similar in both high and low affinity complexes. The differences in affinity correlate with the flexibility of the DNA sequence. Preferences of E2 proteins from different papillomavirus strains for flexible or prevent DNA targets correlate with the distribution of positive charge on their DNA interaction surfaces, suggesting a role for electrostatic forces in the recognition of DNA deformability.

PubMed: 10906136
DOI: 10.1074/jbc.M004541200

実験手法

X-RAY DIFFRACTION (1.9 Å)