Identification of the metal coordinating residues in the DNA binding domain of the glucocorticoid receptor by 113Cd-1H heteronuclear NMR spectroscopy.
FEBS Lett
; 291(2): 367-70, 1991 Oct 21.
Article
em En
| MEDLINE
| ID: mdl-1936288
ABSTRACT
Two-dimensional 1H-113Cd HSQC and relay HSQC experiments were performed on the 113Cd substituted DNA binding domain of the rat glucocorticoid receptor. The results of these experiments combined with sequence-specific assignments allowed the identification of all coordinating cysteines. It was found that C495 and not C500 is the fourth coordinating cysteine in the second zinc-finger. A signal at approximately 2 ppm previously assigned to a epsilon-CH3 of a methionine residue coordinating to a third, weakly bound, cadmium ion, was identified as the C443 beta proton ligating to the metal ion in the first zinc-finger. No indications were found for the presence of a previously suggested third metal ion binding site.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Receptores de Glucocorticoides
/
Proteínas de Ligação a DNA
Tipo de estudo:
Diagnostic_studies
Limite:
Animals
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1991
Tipo de documento:
Article