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'''DNA-BINDING DOMAIN OF FLI-1''' | '''DNA-BINDING DOMAIN OF FLI-1''' | ||
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[[Category: Thompson, C B.]] | [[Category: Thompson, C B.]] | ||
[[Category: Yu, L.]] | [[Category: Yu, L.]] | ||
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Revision as of 13:28, 2 May 2008
DNA-BINDING DOMAIN OF FLI-1
Overview
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.
About this Structure
1FLI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 16:28:02 2008
