Journal article
The secondary structure of the ets domain of human Fli-1 resembles that of the helix-turn-helix DNA-binding motif of the Escherichia coli catabolite gene activator protein
Proceedings of the National Academy of Sciences - PNAS, Vol.91(24), pp.11655-11659
11/22/1994
DOI: 10.1073/pnas.91.24.11655
PMCID: PMC45290
PMID: 7972119
Abstract
The structural characterization of the ets domain of human Fli-1, one member of the ets family of eukaryotic transcription factors, was examined in Escherichia coli. Results suggest that the ets domain is structurally similar to the catabolite gene activator protein family of helix-turn-helix DNA-binding proteins.
Details
- Title: Subtitle
- The secondary structure of the ets domain of human Fli-1 resembles that of the helix-turn-helix DNA-binding motif of the Escherichia coli catabolite gene activator protein
- Creators
- Heng Liang - AbbottEdward Olejniczak - AbbottXiaohong Mao - AbbottDavid Nettesheim - AbbottLiping Yu - Medicine AdministrationCraig B. Thompson - University of ChicagoStephen W. Fesik
- Resource Type
- Journal article
- Publication Details
- Proceedings of the National Academy of Sciences - PNAS, Vol.91(24), pp.11655-11659
- Publisher
- National Academy of Sciences
- DOI
- 10.1073/pnas.91.24.11655
- PMID
- 7972119
- PMCID
- PMC45290
- ISSN
- 0027-8424
- eISSN
- 1091-6490
- Language
- English
- Date published
- 11/22/1994
- Academic Unit
- Biochemistry and Molecular Biology; Medicine Administration
- Record Identifier
- 9984627193602771
Metrics
5 Record Views