Primary structure and expression of a functional human glucocorticoid receptor cDNA
SM Hollenberg, C Weinberger, ES Ong, G Cerelli… - Nature, 1985 - nature.com
SM Hollenberg, C Weinberger, ES Ong, G Cerelli, A Oro, R Lebo, E Brad Thompson…
Nature, 1985•nature.comIdentification of complementary DNAs encoding the human glucocorticoid receptor predicts
two protein forms, of 777 (α) and 742 (β) amino acids, which differ at their carboxy termini.
The proteins contain a cysteine/lysine/arginine-rich region which may define the DNA-
binding domain. Pure radiolabelled glucocorticoid receptor, synthesized in vitro, is immuno-
reactive and possesses intrinsic steroid-binding activity characteristic of the native
glucocorticoid receptor.
two protein forms, of 777 (α) and 742 (β) amino acids, which differ at their carboxy termini.
The proteins contain a cysteine/lysine/arginine-rich region which may define the DNA-
binding domain. Pure radiolabelled glucocorticoid receptor, synthesized in vitro, is immuno-
reactive and possesses intrinsic steroid-binding activity characteristic of the native
glucocorticoid receptor.
Abstract
Identification of complementary DNAs encoding the human glucocorticoid receptor predicts two protein forms, of 777 (α) and 742 (β) amino acids, which differ at their carboxy termini. The proteins contain a cysteine/lysine/arginine-rich region which may define the DNA-binding domain. Pure radiolabelled glucocorticoid receptor, synthesized in vitro, is immuno-reactive and possesses intrinsic steroid-binding activity characteristic of the native glucocorticoid receptor.
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