Solution Structure of the Glucocorticoid Receptor DNA-Binding Domain

Torleif Härd(Utrecht University), Edwin Kellenbach(Utrecht University), Rolf Boelens(Utrecht University), Bonnie A. Maler(University of California, San Francisco), Karin Dahlman(Integrated Cardio Metabolic Centre), Leonard P. Freedman(Memorial Sloan Kettering Cancer Center), Jan Carlstedt‐Duke(Integrated Cardio Metabolic Centre), Keith R. Yamamoto(University of California, San Francisco), Jan-Ακε Gustafsson(Houston Methodist), Robert Kaptein(Utrecht University)
Science
July 13, 1990
Cited by 610

Abstract

The three-dimensional structure of the DNA-binding domain (DBD) of the glucocorticoid receptor has been determined by nuclear magnetic resonance spectroscopy and distance geometry. The structure of a 71-residue protein fragment containing two "zinc finger" domains is based on a large set of proton-proton distances derived from nuclear Overhauser enhancement spectra, hydrogen bonds in previously identified secondary structure elements, and coordination of two zinc atoms by conserved cysteine residues. The DBD is found to consist of a globular body from which the finger regions extend. A model of the dimeric complex between the DBD and the glucocorticoid response element is proposed. The model is consistent with previous results indicating that specific amino acid residues of the DBD are involved in protein-DNA and protein-protein interactions.


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