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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1987 Jul;84(13):4437–4440. doi: 10.1073/pnas.84.13.4437

Domain structure of the glucocorticoid receptor protein.

J Carlstedt-Duke, P E Strömstedt, O Wrange, T Bergman, J A Gustafsson, H Jörnvall
PMCID: PMC305104  PMID: 3474612

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.

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Selected References

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