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Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding
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Evidence for differences in the steroid binding domains of the glucocorticoid receptor versus the idiotype antibody

M K Agarwal, E Cayanis

    Biochemical and Biophysical Research Communications
    |April 29, 1986
    PubMed

    Triamcinolone acetonide (TA), coupled to bovine serum albumin, was used to obtain a polyclonal anti-TA antibody in the rabbit. This idiotype differed from rat glucocorticoid receptor and transcortin in several respects. RU 38486, a synthetic antagonist with high affinity for the receptor, could neither bind the anti-TA antibody nor displace the idiotype bound 3H-TA. Similarly, corticosterone, the natural rodent ligand, had no affinity for the idiotype. These results imply differences in the conformation and topology of the corticoid binding domains, contrary to the current notion where all agonists and antagonists would saturate an identical configuration.

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