Leucine zipper
Leucine Zipper
Leucine Zipper (pronunciation: loo-seen zip-er) is a structural motif in proteins. It is also known as Leucine Scissors due to its characteristic structure.
Etymology
The term "Leucine Zipper" is derived from the amino acid Leucine and the zipper-like pattern that this structure forms. The motif was first identified in 1988.
Definition
A Leucine Zipper is a common three-dimensional structural motif in proteins. It is characterized by a repetitive sequence of Leucine residues at every seventh position, creating an amphipathic alpha helix. These helices can dimerize, forming a coiled-coil structure that resembles a zipper.
Function
Leucine Zippers play a crucial role in DNA binding and protein dimerization, which are essential processes in gene expression. They are found in many transcription factors, where they facilitate the binding of the protein to specific DNA sequences, thereby controlling the transcription of genes.
Related Terms
- Alpha helix
- Amino acid
- DNA binding
- Gene expression
- Leucine
- Protein dimerization
- Transcription factor
External links
- Medical encyclopedia article on Leucine zipper
- Wikipedia's article - Leucine zipper
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