1dto
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(New page: 200px<br /><applet load="1dto" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dto, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 11:27, 20 November 2007
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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.
About this Structure
1DTO is a Single protein structure of sequence from Human papillomavirus type 13. Full crystallographic information is available from OCA.
Reference
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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