Publication Abstract from PubMed
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.
Solution structure of the ets domain of Fli-1 when bound to DNA.,Liang H, Mao X, Olejniczak ET, Nettesheim DG, Yu L, Meadows RP, Thompson CB, Fesik SW Nat Struct Biol. 1994 Dec;1(12):871-5. PMID:7773776[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
