title: Domain structure of the glucocorticoid receptor protein.
abstract: 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.
mesh_terms: 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
chemical_list: D004274:DNA, Recombinant; D004268:DNA-Binding Proteins; D011965:Receptors, Glucocorticoid; D004247:DNA