1qqh
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(New page: 200px<br /><applet load="1qqh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qqh, resolution 2.10Å" /> '''2.1 A CRYSTAL STRUCT...)
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Revision as of 22:46, 20 November 2007
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2.1 A CRYSTAL STRUCTURE OF THE HUMAN PAPILLOMAVIRUS TYPE 18 E2 ACTIVATION DOMAIN
Overview
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 alpha helix packed against a beta-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.
About this Structure
1QQH is a Single protein structure of sequence from Human papillomavirus type 63. Full crystallographic information is available from OCA.
Reference
Crystal structure of the human papillomavirus type 18 E2 activation domain., Harris SF, Botchan MR, Science. 1999 Jun 4;284(5420):1673-7. PMID:10356398
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