Figure 2From: Design of a zinc finger protein binding a sequence upstream of the A20 geneA: Analysis by PepTool Lite indicated that the 176-amino acid sequence of the ZFP involves 6 regularly-aligned, contiguous Cys 2 His 2 -type zinc fingers, which showed the typical β-β-α secondary structure. B: Illustration of 6 contiguous β-β-α zinc fingers constituted the 3-D structural modeling of the backbone of the ZFP, carried out on the online Robetta server. This orderly helical structure would be able to bind specially in the DNA major groove.Back to article page