Identification of the metal coordinating residues in the DNA binding domain of the glucocorticoid receptor by 113Cd‐1H heteronuclear NMR spectroscopy

FEBS Letters

Kaptein, R.¹  Maler, B.A.²  Kellenbach, E.¹  Boelens, R.¹  Yamamoto, K.R.² 

[1] Department of Chemistry, University of Utrecht, Padualaan 8, 3584 CH Utrecht, The Netherlands;Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, CA 94143-0448, USA

关键词: Glucocorticoid receptor DNA binding domain;    113Cd NMR;    Metal coordination;    Zinc-finger;   

DOI  :  10.1016/0014-5793(91)81322-Y

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 ∼2 ppm previously assigned to a ε-CH₃ of a methionine residue coordinating to a third, weakly bound, cadmium ion, was identified as the C443 β 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.

【 授权许可】

Unknown