Structural Analysis of the Glucocorticoid Receptor Protein
Summary
The glucocorticoid receptor protein consists of at least three functional domains. Two of the domains are responsible for the binding of the two different ligands, steroid and DNA, in a coordinated manner. Probing of the structure of the steroid-binding domain by affinity-labelling and radiosequence analysis has identified three steroid-binding amino acid residues in the rat glucocorticoid receptor and two in the human progestin receptor. These residues occur within a hydrophobic surface on this domain. One of the steroid-binding amino acids in the progestin receptor corresponds to the equivalent residue previously identified in the glucocorticoid receptor. The second amino acid identified did not bind steroid in the glucocorticoid receptor. The DNA-binding domain of the human glucocorticoid receptor has been expressed at a high level in E. coli. This protein binds DNA with the same specificity as the intact receptor protein. Two subunits bind to each specific binding site on DNA. The structure and DNA-binding properties of this domain are metal-dependent.
Keywords
Glucocorticoid Receptor Cleavage Method Triamcinolone Acetonide Triamcinolone Acetonide Limited ProteolysisPreview
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