作者: Karin Dahlman-Wright , Kaj Grandien , Stefan Nilsson , Jan-Åke Gustafsson , Jan Carlstedt-Duke
DOI: 10.1016/0960-0760(93)90338-W
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摘要: The glucocorticoid and thyroid hormone receptors have the capacity to bind as dimers palindromic DNA-binding sites. Protein-protein interactions between domains of receptor restrict elements where half-sites are separated by three base pairs, whereas does not appear require a strict half-site spacing. We previously shown that five amino-acid segment close C-terminal zinc-binding site (D-box) was involved in dimerization (GR) domain (Dahlman-Wright et al., 1991, J. Biol. Chem., 266, 3107–3112). Here we provide functional evidence, using mutated domains, this amino acid GR interacts with equivalent on second dimer. In contrast, binds response weakly co-operative manner, independent D-box.