| Literature DB >> 3474612 |
J Carlstedt-Duke, P E Strömstedt, O Wrange, T Bergman, J A Gustafsson, H Jörnvall.
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.Entities:
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Year: 1987 PMID: 3474612 PMCID: PMC305104 DOI: 10.1073/pnas.84.13.4437
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205