Zinc coordination scheme for the C-terminal zinc binding site of nuclear hormone receptors

Johanna Zilliacus, Karin Dahlman-Wright, Jan Carlstedt-Duke, Jan Åke Gustafsson

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


The DNA-binding domain of the glucocorticoid receptor contains two zinc ions which are important for the structure and function of the protein. The zinc ions are tetrahedrally coordinated by cysteine residues within the DNA-binding domain. The DNA-binding domain of the glucocorticoid receptor, as well as of the other nuclear hormone receptors, contains nine highly conserved cysteine residues. It has not been clearly established which of these nine cysteine residues are involved in the coordination of zinc. Two models have been proposed for the zinc coordination scheme. We present evidence in flavour of the model which excludes the most C-terminal cysteine residue (Cys-481 of the human glucocorticoid receptor) from the zinc coordination scheme. Mutation of this residue in the context of the glucocorticoid receptor DNA-binding domain expressed in E. coli does not significantly reduce the structural integrity of the protein or its DNA-binding properties. These in vitro results are also confirmed by in vivo transactivation assays in yeast.

Original languageEnglish (US)
Pages (from-to)131-139
Number of pages9
JournalJournal of Steroid Biochemistry and Molecular Biology
Issue number2
StatePublished - Apr 1992

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Endocrinology
  • Clinical Biochemistry
  • Cell Biology


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