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Updated: Jun 3, 2026
Direct Protein Delivery to Mammalian Cells Using Cell-permeable Cys2-His2 Zinc-finger Domains
Published on: March 25, 2015
A theoretical study of the physicochemical mechanisms associated with DNA recognition modulation in artificial
Hirotoshi Mori1, Kaori Ueno-Noto
1Division of Advanced Sciences, Ocha-dai Academic Production, Ochanomizu University, Tokyo, Japan. mori.hirotoshi@ocha.ac.jp
Abstract:
The DNA-binding ability of the zinc-finger (ZF) protein and the modulation of its affinity to DNA through amino acid mutations were theoretically investigated. Classical molecular dynamics and energy decomposition analysis based on large-scale ab initio fragment molecular orbital calculations were used to obtain the DNA binding affinities of wild-type and three mutant ZFs. Calculated binding free energies qualitatively well explained the DNA binding affinity modulation experimentally observed by Dhanasekaran et al. [Dhanasekaran, M.; et al., Biochemistry 2007, 46, 7506-7513]. It had been considered that only the α-helix domain in the ZF plays an important role in DNA recognition; however, our results clearly show that the N-terminal regions, BR1 and BR2, also play important roles in DNA recognition.
