2NNU

Crystal Structure of the Papillomavirus DNA Tethering Complex E2:Brd4

2NNU の概要

• エントリーDOI: 10.2210/pdb2nnu/pdb
• 分子名称: Regulatory protein E2, Bromodomain-containing protein 4 (3 entities in total)
• 機能のキーワード: protein-peptide complex, helical peptide, three helix bundle, amphipathic helix, transcription
• 由来する生物種: Human papillomavirus type 16; 詳細
• 細胞内の位置: Host nucleus: P03120; Nucleus (By similarity): O60885
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26307.57

構造登録者

Abbate, E.A.,Voitenleitner, C.,Botchan, M.R. (登録日: 2006-10-24, 公開日: 2007-01-09, 最終更新日: 2023-08-30)

主引用文献

Abbate, E.A.,Voitenleitner, C.,Botchan, M.R.
Structure of the Papillomavirus DNA-Tethering Complex E2:Brd4 and a Peptide that Ablates HPV Chromosomal Association.
Mol.Cell, 24:877-889, 2006

PubMed Abstract: Many DNA viruses that are latent in dividing cells are noncovalent passengers on mitotic chromosomes and require specific viral-encoded and cellular factors for this activity. The chromosomal protein Brd4 is implicated in the hitchhiking of bovine papillomavirus-1 (BPV-1), and the viral protein E2 binds to both plasmids and Brd4. Here, we present the X-ray crystal structure of the carboxy-terminal domain of Brd4 in complex with HPV-16 E2, and with this information have developed a Brd4-Tat fusion protein that is efficiently taken up by different transformed cells harboring HPV plasmids. In cells treated with these fusion proteins for only 2 hr and arrested in metaphase, the HPV DNA, either HPV-16 or -31, is displaced from mitotic chromosomes. Mutant Brd4 peptides are deficient in ablating this association. We suggest that such peptides may lead to the development of inhibitors of latency for many, if not all, papillomaviruses.

PubMed: 17189190
DOI: 10.1016/j.molcel.2006.11.002

実験手法

X-RAY DIFFRACTION (1.59 Å)