Abstract
STEROID hormone receptors control gene expression through binding, as dimers, to short palindromic response elements located upstream of the genes they regulate1–3. An independent domain of ∼70 amino acids directs this sequence-specific DNA binding and is highly conserved between different receptor proteins and related transcription factors4–6. This domain contains two zinc-binding Cys2–Cys2 sequence motifs, which loosely resemble the 'zinc-finger' motifs of TFIIIA7–10. Here we describe the structure of the DNA-binding domain from the oestrogen receptor, as determined by two-dimensional 1H NMR techniques. The two 'zinc-finger'-like motifs fold to form a single structural domain and are thus distinct from the independently folded units of the TFIIIA-type zinc fingers11–13. The structure consists of two helices perpendicular to each other. A zinc ion, coordinated by four conserved cysteines, holds the base of a loop at the N terminus of each helix. This novel structural domain seems to be a general structure for protein-DNA recognition.
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Schwabe, J., Neuhaus, D. & Rhodes, D. Solution structure of the DMA-binding domain of the oestrogen receptor. Nature 348, 458–461 (1990). https://doi.org/10.1038/348458a0
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DOI: https://doi.org/10.1038/348458a0
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