Zinc finger

Zinc Finger

Zinc Finger (pronunciation: /zɪŋk ˈfɪŋɡər/) is a small protein structural motif that is characterized by the coordination of one or more zinc ions in order to stabilize the fold.

Etymology

The term "Zinc Finger" was coined due to the unique finger-like shape of the protein structure when a zinc ion is coordinated with the protein. The zinc ion is typically coordinated with cysteine and histidine residues in the protein.

Structure

Zinc fingers are small protein domains in which a zinc ion is coordinated with usually four amino acid residues, often cysteine and histidine. The zinc ion serves to stabilize the fold of the protein domain, allowing it to interact with other molecules.

Function

Zinc fingers are found in many proteins and are involved in a variety of functions, including DNA recognition, RNA packaging, transcriptional activation, regulation of apoptosis, protein folding and assembly, and lipid binding.

Related Terms

• Protein Structure
• Cysteine
• Histidine
• DNA Recognition
• RNA Packaging
• Transcriptional Activation
• Regulation of Apoptosis
• Protein Folding
• Lipid Binding

External links

• Medical encyclopedia article on Zinc finger
• Wikipedia's article - Zinc finger

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