Journal article
Solution structure of the ets domain of Fli-1 when bound to DNA
Nature structural & molecular biology, Vol.1(12), pp.871-876
12/01/1994
DOI: 10.1038/nsb1294-871
PMID: 7773776
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 α-helices and a four-stranded β-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.
Details
- Title: Subtitle
- Solution structure of the ets domain of Fli-1 when bound to DNA
- Creators
- Heng Liang - Discovery LaboratoriesXiaohong Mao - University of ChicagoEdward T. Olejniczak - AbbottDavid G. Nettesheim - Discovery LaboratoriesLiping Yu - Discovery LaboratoriesRobert P. Meadows - Discovery LaboratoriesCraig B. Thompson - University of ChicagoStephen W. Fesik - Discovery Laboratories
- Resource Type
- Journal article
- Publication Details
- Nature structural & molecular biology, Vol.1(12), pp.871-876
- DOI
- 10.1038/nsb1294-871
- PMID
- 7773776
- ISSN
- 1545-9993
- eISSN
- 1545-9985
- Language
- English
- Date published
- 12/01/1994
- Academic Unit
- Biochemistry and Molecular Biology; Medicine Administration
- Record Identifier
- 9984627202802771
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