Report

Crystal Structure of the Human Papillomavirus Type 18 E2 Activation Domain

Science  04 Jun 1999:
Vol. 284, Issue 5420, pp. 1673-1677
DOI: 10.1126/science.284.5420.1673

You are currently viewing the abstract.

View Full Text
As a service to the community, AAAS/Science has made this article free with registration.

This article has a correction. Please see:

Abstract

The papillomavirus E2 protein regulates viral transcription and DNA replication through interactions with cellular and viral proteins. The amino-terminal activation domain, which represents a protein class whose structural themes are poorly understood, contains key residues that mediate these functional contacts. The crystal structure of a protease-resistant core of the human papillomavirus type 18 E2 activation domain reveals a novel fold creating a cashew-shaped form with a glutamine-rich α helix packed against a β-sheet framework. The protein surface shows extensive overlap of determinants for replication and transcription. The structure broadens the concept of activators to include proteins with potentially malleable, but certainly ordered, structures.

  • * To whom correspondence should be addressed. E-mail: mbotchan{at}uclink4.berkeley.edu

View Full Text

Cited By...