Document Detail


Functional probing of glucocorticoid receptor structure.
MedLine Citation:
PMID:  3059058     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The glucocorticoid receptor (GR) consists of three functional domains. The steroid-binding domain is situated at the C-terminal end and N-terminal sequence analysis has identified the border of this domain at residue 518. The DNA-binding domain is central and lies between residues 414 and 517. The remaining N-terminal half of the protein constitutes the third domain. Probing of the steroid-receptor interaction by affinity-labelling and radiosequence analysis has identified three steroid-binding amino acid residues, Met-622, Cys-656 and Cys-754.
Authors:
J Carlstedt-Duke; J A Gustafsson
Related Documents :
10751638 - Synthesis and biological activity of a new progestogen, 16-methylene-17alpha-hydroxy-18...
8439518 - Binding affinities of mometasone furoate and related compounds including its metabolite...
2752988 - Characterization of the corticosteroid-binding globulin response to decidualization in ...
3990518 - Epinephrine and norepinephrine syntheses are regulated by a glucocorticoid receptor-med...
2230238 - Cefuroxime treatment failure of nontypable haemophilus influenzae meningitis associated...
23275688 - Insights from the predicted interactions of plant derived compounds to the gluco-cortic...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Journal of steroid biochemistry     Volume:  31     ISSN:  0022-4731     ISO Abbreviation:  J. Steroid Biochem.     Publication Date:  1988 Oct 
Date Detail:
Created Date:  1989-01-19     Completed Date:  1989-01-19     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0260125     Medline TA:  J Steroid Biochem     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  593-7     Citation Subset:  IM    
Affiliation:
Department of Medical Nutrition, Karolinska Institute, Huddinge University Hospital, Sweden.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Binding Sites
DNA-Binding Proteins / physiology
Glucocorticoids / metabolism
Molecular Weight
Nuclear Proteins / ultrastructure*
Peptide Hydrolases / metabolism
Receptors, Glucocorticoid / physiology,  ultrastructure*
Regulatory Sequences, Nucleic Acid
Chemical
Reg. No./Substance:
0/DNA-Binding Proteins; 0/Glucocorticoids; 0/Nuclear Proteins; 0/Receptors, Glucocorticoid; EC 3.4.-/Peptide Hydrolases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Nuclear acceptor sites for steroid hormone receptors: comparisons of steroids and antisteroids.
Next Document:  Pharmacodynamic and biological effects of anti-estrogens in different models.