A helix-turn-helix motif characterized by three alpha-helices and four-stranded beta-sheets arranged in the order alpha1-beta1-beta2-alpha2-alpha3-beta3-beta4. The third alpha-helix contacts the major groove of DNA. The ETS motif and the flanking amino acid sequences of Ets proteins influence the binding affinity, and the alteration of a single amino acid in the Ets domain can change its DNA binding specificity.
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