China
Africa
Explore chapters and articles related to this topic
Gene Therapy and Gene Correction
Published in Yashwant V. Pathak, Gene Delivery Systems, 2022
Manish P. Patel, Sagar A. Popat, Jayvadan K. Patel
ZFNs are already being approved for clinical trial testing (Muenzer et al. 2019). Initially ZFNs were developed based on the ability of zinc-finger transcription factors to recognize a DNA sequence. Zinc-finger proteins have a sequence for DNA-binding activity, which are specific for each gene (Bibikova et al. 2001). The first study was carried out to produce a chimeric protein by hybridizing the zinc-finger domain with a nuclease. It produced a sequence-specific double-strand break (Rouet et al. 1994).
Structures
Published in Thomas M. Nordlund, Peter M. Hoffmann, Quantitative Understanding of Biosystems, 2019
Thomas M. Nordlund, Peter M. Hoffmann
Many molecules critical to life are not listed in Table 5.1 because their amounts are so tiny. We will not dwell on this subject, but it is interesting to note that some atoms and molecules occurring in humans in trace quantities are both required nutrients and poisons, depending on the amount.4 Examples among the transition metals include chromium, copper, manganese, zinc, and even iron. These elements are often needed because they take part in oxidation-reduction reactions involved in cellular respiration, chemical detoxification, metabolism, and neurotransmitter synthesis. We will also see zinc playing a central role in DNA-binding proteins, in a role referred to as zinc fingers. However, elements such as lead and cadmium may be metabolized like iron, cannot play the same biochemical role as iron, and act strictly as poisons.
Glossary of scientific and technical terms in bioengineering and biological engineering
Published in Megh R. Goyal, Scientific and Technical Terms in Bioengineering and Biological Engineering, 2018
Zinc finger is a DNA-binding protein motif, characterized by two closely spaced cysteine and two histidine residues that serve as ligands for a single Zn2+ ion. When bound, the structure takes on a conformation in which amino acid side chains protrude in a way that allows interaction with the DNA major groove.
Expression, purification, and characterization of N-terminal His-tagged proteins with mutations in zinc finger 3 of zinc finger protein ZNF191(243–368)
Published in Preparative Biochemistry and Biotechnology, 2018
Dongxin Zhao, Zhongxian Huang, Jie Liu, Li Ma, Juan He
In the Krüppel-type zinc finger domain, the coordination of zinc ions with two Cys and two His residues in the zinc finger peptide facilitates the formation of a tetrahedral structure, which is necessary for maintaining the function of the zinc finger protein. Destruction of the spatial structure of the zinc finger domain by dezincification and recovery by the addition of zinc ions confirmed that zinc ions promote the folding of the zinc finger peptide chain. CD spectroscopy is an effective means to test the folding of the zinc finger and depends on the zinc ion coordination.[17]