1dto: Difference between revisions

Revision as of 23:36, 30 June 2008

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File:1dto.png

Template:STRUCTURE 1dto

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

Template:ABSTRACT PUBMED 10693813

About this StructureAbout this Structure

1DTO is a Single protein structure of sequence from Human papillomavirus type 16. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the intact transactivation domain of the human papillomavirus E2 protein., Antson AA, Burns JE, Moroz OV, Scott DJ, Sanders CM, Bronstein IB, Dodson GG, Wilson KS, Maitland NJ, Nature. 2000 Feb 17;403(6771):805-9. PMID:10693813

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''CRYSTAL STRUCTURE OF THE COMPLETE TRANSACTIVATION DOMAIN OF E2 PROTEIN FROM THE HUMAN PAPILLOMAVIRUS TYPE 16'''
+===CRYSTAL STRUCTURE OF THE COMPLETE TRANSACTIVATION DOMAIN OF E2 PROTEIN FROM THE HUMAN PAPILLOMAVIRUS TYPE 16===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10693813}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10693813 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10693813}}
 ==About this Structure==
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 [[Category: Beta-sheet]]
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