Domain structure of the glucocorticoid receptor protein.

J. Carlstedt-Duke, P. E. Strömstedt, O. Wrange, T. Bergman, J. A. Gustafsson, H. Jörnvall

Research output: Contribution to journalArticlepeer-review

92 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)4437-4440
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number13
StatePublished - Jul 1987

ASJC Scopus subject areas

  • General


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