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Structural characte...
Structural characterization of a minimal functional transactivation domain from the human glucocorticoid receptor
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DAHLMANWRIGHT, K (author)
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BAUMANN, H (author)
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MCEWAN, IJ (author)
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ALMLOF, T (author)
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- WRIGHT, APH (author)
- Karolinska Institutet
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- GUSTAFSSON, JA (author)
- Karolinska Institutet
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HARD, T (author)
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(creator_code:org_t)
- 1995-02-28
- 1995
- English.
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In: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 0027-8424. ; 92:5, s. 1699-1703
- Related links:
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http://www.pnas.org/...
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http://kipublication...
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https://doi.org/10.1...
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Abstract
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- A 58-amino acid polypeptide containing the functional core region, the tau 1 core, of the major transactivation domain of the human glucocorticoid receptor has been expressed in Escherichia coli and purified to homogeneity. The polypeptide retains 60-70% of the activity of the intact domain when assayed in vivo or in vitro. This report describes a structural characterization of the tau 1 core peptide fragment. Circular dichroism spectroscopy shows that the tau 1 core and a larger fragment encompassing the intact tau 1 domain are largely unstructured in water solution under a variety of pH conditions. The tau 1 core, however, acquires a significant alpha-helical structure when analyzed in the presence of trifluoroethanol, an agent that favors secondary structure formation in regions that have propensity for alpha-helical conformation. Two- and three-dimensional NMR spectroscopy of 15N-labeled tau 1 core, in the presence of trifluoroethanol, has allowed sequential assignment of 1H and 15N resonances and identification of three protein segments with alpha-helical character. Potentially helix-breaking proline substitutions, in proposed alpha-helical regions, lead to reduced activity, suggesting that alpha-helices are important for transactivation in vivo.
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