Solution structure of the DMA-binding domain of the oestrogen receptor (original) (raw)

Nature volume 348, pages 458–461 (1990)Cite this article

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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Authors and Affiliations

  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK
    John W. R. Schwabe, David Neuhaus & Daniela Rhodes

Authors

  1. John W. R. Schwabe
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  2. David Neuhaus
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  3. Daniela Rhodes
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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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