1DTO

CRYSTAL STRUCTURE OF THE COMPLETE TRANSACTIVATION DOMAIN OF E2 PROTEIN FROM THE HUMAN PAPILLOMAVIRUS TYPE 16

1DTO の概要

• エントリーDOI: 10.2210/pdb1dto/pdb
• 分子名称: REGULATORY PROTEIN E2 (2 entities in total)
• 機能のキーワード: three-helix bundle, beta-sheet, viral protein
• 由来する生物種: Human papillomavirus type 16
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25698.96

構造登録者

Antson, A.A.,Burns, J.E.,Moroz, O.V.,Scott, D.J.,Sanders, C.M.,Bronstein, I.B.,Dodson, G.G.,Wilson, K.S.,Maitland, N. (登録日: 2000-01-13, 公開日: 2000-02-23, 最終更新日: 2024-02-07)

主引用文献

Antson, A.A.,Burns, J.E.,Moroz, O.V.,Scott, D.J.,Sanders, C.M.,Bronstein, I.B.,Dodson, G.G.,Wilson, K.S.,Maitland, N.J.
Structure of the intact transactivation domain of the human papillomavirus E2 protein.
Nature, 403:805-809, 2000

PubMed Abstract: Papillomaviruses cause warts and proliferative lesions in skin and other epithelia. In a minority of papillomavirus types ('high risk, including human papillomaviruses 16, 18, 31, 33, 45 and 56), further transformation of the wart lesions can produce tumours. The papillomavirus E2 protein controls primary transcription and replication of the viral genome. Both activities are governed by a approximately 200 amino-acid amino-terminal module (E2NT) which is connected to a DNA-binding carboxy-terminal module by a flexible linker. Here we describe the crystal structure of the complete E2NT module from human papillomavirus 16. The E2NT module forms a dimer both in the crystal and in solution. Amino acids that are necessary for transactivation are located at the dimer interface, indicating that the dimer structure may be important in the interactions of E2NT with viral and cellular transcription factors. We propose that dimer formation may contribute to the stabilization of DNA loops which may serve to relocate distal DNA-binding transcription factors to the site of human papillomavirus transcription initiation.

PubMed: 10693813
DOI: 10.1038/35001638

実験手法

X-RAY DIFFRACTION (1.9 Å)