TY - JOUR
T1 - Domain structure of the glucocorticoid receptor protein.
AU - Carlstedt-Duke, J.
AU - Strömstedt, P. E.
AU - Wrange, O.
AU - Bergman, T.
AU - Gustafsson, J. A.
AU - Jörnvall, H.
PY - 1987/7
Y1 - 1987/7
N2 - 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.
AB - 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.
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U2 - 10.1073/pnas.84.13.4437
DO - 10.1073/pnas.84.13.4437
M3 - Article
C2 - 3474612
AN - SCOPUS:0023372378
VL - 84
SP - 4437
EP - 4440
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 13
ER -