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
This WikiMD article is a stub. You can help make it a full article.
Languages: - East Asian
中文,
日本,
한국어,
South Asian
हिन्दी,
Urdu,
বাংলা,
తెలుగు,
தமிழ்,
ಕನ್ನಡ,
Southeast Asian
Indonesian,
Vietnamese,
Thai,
မြန်မာဘာသာ,
European
español,
Deutsch,
français,
русский,
português do Brasil,
Italian,
polski