SOLUTION STRUCTURE OF THE ETS DOMAIN OF FLI-1 WHEN BOUND TO DNA

Members of the ets family of transcription factors share a conserved D NA-binding domain, the ets domain. By using multidimensional NMR we ha ve determined the structure of the ets domain of human Fli-1 in the DN A-bound form. It consists of three a-helices and a four-stranded beta- sheet, similar to structures of the class of helix-turn-helix DNA bind ing proteins first found in the catabolite activator protein of Escher ichia 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.