| Literature DB >> 1841686 |
E Kellenbach1, T Härd, R Boelens, K Dahlman, J Carlstedt-Duke, J A Gustafsson, G A van der Marel, J H van Boom, B Maler, K R Yamamoto.
Abstract
Photo-CIDNP studies were performed on two protein fragments that both contain the double zinc-finger DNA-binding domain of the glucocorticoid receptor. In the absence of DNA, Tyr452 and Tyr474 are polarised in both fragments while Tyr497 is not. Addition of a palindromic glucocorticoid response element (GRE) results in the suppression of Tyr474 polarization while the polarization of Tyr452 is unaffected. The same result is observed upon adding a half GRE to the protein fragment indicating that the suppression of Tyr474 polarization is not due to protein-protein contacts but to interaction with DNA.Entities:
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Year: 1991 PMID: 1841686 DOI: 10.1007/bf01874574
Source DB: PubMed Journal: J Biomol NMR ISSN: 0925-2738 Impact factor: 2.835