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Updated: Jul 24, 2026

Direct Protein Delivery to Mammalian Cells Using Cell-permeable Cys2-His2 Zinc-finger Domains
Published on: March 25, 2015
[Prospects for realizing a structure of the spiral-turn-spiral type in a "zinc finger"]
Abstract:
The realization of two models for Zn-finger structure--DNA-binding domain was estimated by taking into account the geometric and energetic requirements of polypeptide chain folding. The following structures were taken as models: antiparallel beta-structure and helix-turn-helix motif. The latter hasn't been considered earlier as the possible structure for Zn-finger. The preference was given to the above-mentioned models on the base of the available experimental data. It was shown that the helix-turn-helix motif for which the angle between axes of alpha-helices doesn't exceed 40 degrees cannot be excluded from the list of the assumed models for Zn-finger. There is a suggestion that the helix-turn-helix motif is likely to be characteristic for the majority of DNA-binding domains in proteins.
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