2F8B

NMR structure of the C-terminal domain (dimer) of HPV45 oncoprotein E7

2F8B の概要

• エントリーDOI: 10.2210/pdb2f8b/pdb
• 関連するPDBエントリー: 2EWL
• NMR情報: BMRB: 6916
• 分子名称: Protein E7, ZINC ION (2 entities in total)
• 機能のキーワード: e7, dimer, hpv, oncoprotein, zinc binding, virus-viral protein complex, virus/viral protein
• 由来する生物種: Human papillomavirus type 45
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 12741.40

構造登録者

Ohlenschlager, O.,Gorlach, M. (登録日: 2005-12-02, 公開日: 2006-08-08, 最終更新日: 2024-05-29)

主引用文献

Ohlenschlager, O.,Seiboth, T.,Zengerling, H.,Briese, L.,Marchanka, A.,Ramachandran, R.,Baum, M.,Korbas, M.,Meyer-Klaucke, W.,Durst, M.,Gorlach, M.
Solution structure of the partially folded high-risk human papilloma virus 45 oncoprotein E7.
Oncogene, 25:5953-5959, 2006

PubMed Abstract: The oncoprotein E7 of human papilloma viruses (HPV) is involved in the pathogenesis and maintenance of human cervical cancers. The most prevalent HPV types found in cervix carcinomas are HPV16, 18 and 45. The structure of the E7 dimer from HPV45 (PDB 2F8B) was determined by nuclear magnetic resonance spectroscopy. Each monomer comprises an unfolded N-terminus and a well-structured C-terminal domain with a beta1beta2alpha1beta3alpha2 topology representing a unique zinc-binding fold found only for E7. Dimerization occurs through the alpha1/alpha1' helices and intermolecular beta-sheet formation but excludes the zinc-binding sites. E7 is reported to interact with a number of cellular proteins (e.g. pRb, p21(CIP1)). Binding of a peptide derived from the C-terminus of p21(CIP1) to the C-terminal domain of E7 was characterized by monitoring chemical shift perturbations of the amide groups of E7. This provides direct evidence that a shallow groove situated between alpha1 and beta1 of the E7 C-terminal domain is interacting with the C-terminus of p21(CIP1). Intriguingly, this binding site overlaps with the low-affinity binding site on E7 for the C-domain of pRb.

PubMed: 16636661
DOI: 10.1038/sj.onc.1209584

実験手法

SOLUTION NMR