WebZIF268, a member of the classical zinc finger protein family, contains three Cys2His2 zinc binding domains that together recognize the DNA sequence 5′-AGCGTGGGCGT-3′. … WebJan 9, 2024 · So far, zinc finger motifs have been classified into eight different categories according to their main-chain conformation and secondary structure around their zinc-binding sites, including Cys2His2 (C2H2) like, Zn2/Cys6, Treble clef, Zinc ribbon, Gag knuckle, TAZ2 domain like, Zinc binding loops and Metallothionein [3, 4]. In addition to …
DNA Recognition by Cys2His2 Zinc Finger Proteins
WebMay 30, 2007 · The Cys2His2 zinc finger is the most abundant class of DNA-binding domain found in human transcription factors ( 1). The considerable expansion of this domain in higher eukaryotes is likely related to its modularity and to its ability to specify a diverse range of different DNA sequences. WebMar 1, 2012 · Cys2His2 (C2H2)-type zinc fingers are widespread DNA binding motifs in eukaryotic transcription factors. Zinc fingers are short protein motifs composed of two or … css grid column responsive
Cys2His2 Zinc Finger Proteins - UMass Chan Medical School
WebFeb 23, 2024 · The Cys2His2 ZFPs can specifically bind DNA only in their Zn (II)-bound form. The coordination of Zn (II) to 2 cysteine and 2 histidine amino acid sidechains induces the protein folding into a characteristic ββα secondary structure. Therefore, their metal ion affinity is crucial in Zn (II) sequestering and proper functioning. WebMay 19, 2024 · Cys2His2 zinc finger (ZF-Cys2His2) proteins have been found in a number of plants including Arabidopsis, cotton, rice and wheat. The ZF-Cys2His2 is built by two Cys and two His residues. This structure provides a conservative motif together with Zn 2+. WebAbstract Cys 2 His 2 zinc finger proteins offer a stable and versatile framework for the design of proteins that recognize desired target sites on double-stranded DNA. Individual … earl forrest last meal