Creation of "super" glucocorticoid receptors by point mutations in the steroid binding domain

Chakraborti, P. K. ; Garabedian, M. J. ; Yamamoto, K. R. ; Simons, S. S. (1991) Creation of "super" glucocorticoid receptors by point mutations in the steroid binding domain Journal of Biological Chemistry, 266 (33). pp. 22075-22078. ISSN 0021-9258

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Official URL: http://www.jbc.org/content/266/33/22075.abstract

Abstract

Almost all modifications of the steroid binding domain of glucocorticoid receptors are known to cause a reduction or loss of steroid binding activity. Nonetheless, we now report that mutations of cysteine 656 of the rat receptor, which was previously suspected to be a crucial amino acid for the binding process, have produced "super" receptors. These receptors displayed an increased affinity for glucocorticoid steroids and a decreased relative affinity for cross-reacting steroids such as progesterone and aldosterone. The increased in vitro affinity of the super receptors was maintained in a whole cell bioassay. These results indicate that additional modifications of the glucocorticoid receptor, and probably the other steroid receptors, may further increase the binding affinity and/or specificity.

Item Type:Article
Source:Copyright of this article belongs to The American Society for Biochemistry and Molecular Biology.
ID Code:60368
Deposited On:08 Sep 2011 14:35
Last Modified:08 Sep 2011 14:35

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