Domain structure of the glucocorticoid receptor protein.
The purified rat liver glucocorticoid receptor protein was analyzed by limited proteolysis and amino acid sequence determination. The NH2 terminus appears to be blocked. The steroid-binding domain, defined by a unique tryptic cleavage site, corresponds to the COOH-terminal part of the protein with the domain border in the region of residue 518. The DNA-binding domain, defined by a region with chymotryptic cleavage sites, is immediately adjacent to the steroid-binding domain and reflects another domain border in the region of residues 410-414. The results described at the protein level in this report confirm functional data previously obtained by mutations at the genetic level.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D004247:DNA / Q000235:genetics; D004274:DNA, Recombinant; D004268:DNA-Binding Proteins / Q000235:genetics; D008099:Liver / Q000032:analysis; D011485:Protein Binding; D011487:Protein Conformation; D051381:Rats; D011965:Receptors, Glucocorticoid / Q000235:genetics
D004274:DNA, Recombinant; D004268:DNA-Binding Proteins; D011965:Receptors, Glucocorticoid; D004247:DNA