zincfingerdomäner
Zinc finger domains are protein structural motifs that are crucial for the function of many transcription factors and other DNA-binding proteins. These domains are characterized by their ability to coordinate one or more zinc ions, which stabilize the protein's folded structure. The zinc ions are typically held in place by a specific arrangement of cysteine and/or histidine residues. This zinc-binding capability is essential for the protein to fold into a three-dimensional shape that allows it to interact with DNA.
The most common type of zinc finger is the Cys2His2 (C2H2) zinc finger. In this type, two
Zinc finger domains play critical roles in gene regulation. They are key components of transcription factors