Fli-1, DNA-Binding Domain

Human Fli-1 is a member of the ets family of transcription factors that share a conserved region. This region is the DNA-binding domain, or ets domain. This conserved domain is approximately 85 amino acid residues long. Structurally, the DNA-binding domain of Fli-1 consists of 3 alpha-helices (purple), 2 antiparallel beta-strands (magenta), and a single 310 alpha helix (gold). This molecular architecture is similar to the helix-turn-helix motif of DNA-binding proteins. The secondary structure of the Fli-1 DNA-binding domain is similar to the DNA-binding domain of the catabolite gene activator protein of Escherichia coli.
Fli-1 is a sequence specific transcriptional activator. It recognizes the DNA sequence 5'-C(CA)GGAAGT-3'. The DNA-binding domain of human Fli-1 is 98 amino acid residues long.


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