Solution structure of the DNA-binding domain of the oestrogen receptor.

摘要: 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 ∼70 amino acids directs this sequence-specific DNA binding and is highly conserved between different receptor proteins related transcription factors4–6. This contains two zinc-binding Cys2–Cys2 sequence motifs, which loosely resemble 'zinc-finger' motifs TFIIIA7–10. Here we describe structure DNA-binding from oestrogen receptor, determined by two-dimensional 1H NMR techniques. The 'zinc-finger'-like fold form a single structural are thus distinct independently folded units TFIIIA-type zinc fingers11–13. consists helices perpendicular each other. A ion, coordinated four cysteines, holds base loop at N terminus helix. novel seems be general for protein-DNA recognition.