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. 1994 Dec;1(12):871-5.
doi: 10.1038/nsb1294-871.

Solution structure of the ets domain of Fli-1 when bound to DNA

H Liang  1 , X Mao, E T Olejniczak, D G Nettesheim, L Yu, R P Meadows, C B Thompson, S W Fesik
Affiliations

Solution structure of the ets domain of Fli-1 when bound to DNA

H Liang et al. Nat Struct Biol. 1994 Dec.

Abstract

Members of the ets family of transcription factors share a conserved DNA-binding domain, the ets domain. By using multidimensional NMR, we have determined the structure of the ets domain of human Fli-1 in the DNA-bound form. It consists of three alpha-helices and a four-stranded beta-sheet, similar to structures of the class of helix-turn-helix DNA binding proteins first found in the catabolite activator protein of Escherichia coli. NMR and mutagenesis experiments suggest that in comparison to structurally related proteins, the ets domain uses a new variation of the helix-turn-helix motif for binding to DNA.

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