The C7.GAT protein is a

zinc finger protein A zinc finger is a small protein structural motif that is characterized by the coordination of one or more zinc ions (Zn2+) in order to stabilize the fold. It was originally coined to describe the finger-like appearance of a hypothesized structu ...

based on the

C7 protein C7 protein is an engineered zinc finger protein based on the murine ZFP, Zif268 and discovered by Wu ''et al.'' in 1994 (published in 1995). It shares the same zinc finger 2 and zinc finger 3 of Zif268, but differs in the sequence of finger 1. It a ...

(itself based on the murine Zif268). It features an alternative zinc finger 3

alpha helix The alpha helix (α-helix) is a common motif in the secondary structure of proteins and is a right hand-helix conformation in which every backbone N−H group hydrogen bonds to the backbone C=O group of the amino acid located four residues e ...

sequence, preventing the target site overlap caused by the

aspartic acid Aspartic acid (symbol Asp or D; the ionic form is known as aspartate), is an α-amino acid that is used in the biosynthesis of proteins. Like all other amino acids, it contains an amino group and a carboxylic acid. Its α-amino group is in the pro ...

residue of the finger 3 of C7. The sequence of this third finger is TSG-N-LVR according to the single letter amino acid code. As the name suggest, the target site of finger 3 is altered to 5'-GAT-3', giving the overall protein a target of 5'-GCGTGGGAT-3'. C7.GAT is used in studies investigating the effects of altering zinc finger alpha helix sequence on the target of the altered zinc finger, as well as the affinity and specificity of these proteins to their targets.

References

* {{DEFAULTSORT:C7.Gat Protein Engineered proteins Genetics experiments Molecular genetics