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• W291220406 abstract "The effects of steroids on the binding of [1,2-3H]dexamethasone and [1,2-3H]progesterone to the glucocorticoid receptor of rat thymus cytosol were studied. Although both glucocorticoid agonists and antagonists competed with [1,2-3H]dexamethasone for binding to the receptor under equilibrium conditions, only glucocorticoid antagonists of partial agonists, at micromolar concentrations, were capable of accelerating the rate of dissociation of previously bound [1,2-3H]dexamethasone from the receptor. Antagonists or partial agonists also enhanced the rate of dissociation of [1,2-3H]progesterone from the glucocorticoid receptor, with identical specificity and concentration–response characteristics. These effects are attributed to the presence on the receptor of a secondary, low-affinity, binding site for glucocorticoid antagonists, the occupancy of which produces negatively co-operative interactions with the primary glucocorticoid-binding site. In contrast with the interactions with the primary site, the interactions of steroids with the negatively co-operative site appear to be primarily hydrophobic in nature, and the site resembles the steroid-binding site of progestin-binding proteins in its specificity, though not its affinity. The results also suggest that the initial interactions of both glucocorticoid agonists and antagonists with the receptor under equilibrium conditions are with one primary site on a receptor existing in one conformation only." @default.
• W291220406 created "2016-06-24" @default.
• W291220406 creator A5008888304 @default.
• W291220406 creator A5027754866 @default.
• W291220406 date "1980-04-15" @default.
• W291220406 modified "2023-09-26" @default.
• W291220406 title "Glucocorticoid-receptor interactions. Studies of the negative co-operativity induced by steroid interactions with a secondary, hydrophobic, binding site" @default.
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• W291220406 doi "https://doi.org/10.1042/bj1880237" @default.
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