Identification of hormone-interacting amino acid residues within the steroid-binding domain of the glucocorticoid receptor in relation to other steroid hormone receptors
Purified rat liver glucocorticoid receptor was covalently charged with (/sup 3/H)glucocorticoid by photoaffinity labeling (UV irradiation of (/sup 3/H)triamcinolone acetonide-glucocorticoid receptor) or affinity labeling (incubation with (/sup 3/H)dexamethasone mesylate). After labeling, separate samples of the denatured receptor were cleaved with trypsin (directly or after prior succinylation), chymotrypsin, and cyanogen bromide. Labeled residues in the peptides obtained were identified by radiosequence analysis. The peaks of radioactivity corresponded to Met-622 and Cys-754 after photoaffinity labeling with (/sup 3/H)triamcinolone acetonide and Cys-656 after affinity labeling with (/sup 3/H)dexamethasone mesylate. The labeled residues are all positioned within hydrophobic segments of the steroid-binding domain. The patterns of hydropathy and secondary structure for the glucocorticoid receptor are highly similar to those for the progestin receptor and similar but less so to those for the estrogen receptor and to those for c-erb A.
- Research Organization:
- Karolinska Institutet, Huddinge (Sweden)
- OSTI ID:
- 6925125
- Journal Information:
- J. Biol. Chem.; (United States), Vol. 263:14
- Country of Publication:
- United States
- Language:
- English
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GLUCOCORTICOIDS
CONFIGURATION INTERACTION
RECEPTORS
AMINO ACID SEQUENCE
TRITIUM COMPOUNDS
CHEMISTRY
DNA
EXTREME ULTRAVIOLET RADIATION
LIGANDS
LIVER
RATS
ADRENAL HORMONES
ANIMALS
BODY
CORTICOSTEROIDS
DIGESTIVE SYSTEM
ELECTROMAGNETIC RADIATION
GLANDS
HYDROXY COMPOUNDS
KETONES
LABELLED COMPOUNDS
MAMMALS
MEMBRANE PROTEINS
MOLECULAR STRUCTURE
NUCLEIC ACIDS
ORGANIC COMPOUNDS
ORGANS
PREGNANES
PROTEINS
RADIATIONS
RODENTS
STEROIDS
ULTRAVIOLET RADIATION
VERTEBRATES
550201* - Biochemistry- Tracer Techniques