1FLI
DNA-BINDING DOMAIN OF FLI-1
Summary for 1FLI
Entry DOI | 10.2210/pdb1fli/pdb |
Descriptor | FLI-1 (1 entity in total) |
Functional Keywords | transcription/dna, transcription-dna complex |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus: Q01543 |
Total number of polymer chains | 1 |
Total formula weight | 11444.93 |
Authors | Liang, H.,Mao, X.,Olejniczak, E.T.,Nettesheim, D.G.,Yu, L.,Meadows, R.P.,Thompson, C.B.,Fesik, S.W. (deposition date: 1994-09-15, release date: 1995-09-15, Last modification date: 2024-05-22) |
Primary citation | Liang, H.,Mao, X.,Olejniczak, E.T.,Nettesheim, D.G.,Yu, L.,Meadows, R.P.,Thompson, C.B.,Fesik, S.W. Solution structure of the ets domain of Fli-1 when bound to DNA. Nat.Struct.Biol., 1:871-875, 1994 Cited by PubMed 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. PubMed: 7773776DOI: 10.1038/nsb1294-871 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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