Leucine zipper

Leucine zipper is a common three-dimensional structural motif in proteins. It is named for leucines that occur every seven amino acids in the dimerization domain. The leucine zipper is a type of protein motif that stabilizes the protein, specifically the dimerization domain.

Structure[edit | edit source]

The leucine zipper is characterized by leucines occurring every seven amino acids, appearing to form a "zipper" in the protein structure. The leucines are located on the same side of the alpha helices, and when the helices dimerize, the leucines interlock, just like the teeth of a zipper. This structure is also known as a coiled coil.

Function[edit | edit source]

The leucine zipper motif is used by many regulatory proteins that function by binding to DNA. The motif is a part of the DNA-binding domain of the protein, which allows the protein to recognize and bind to specific sequences of DNA. This binding can regulate the transcription of genes, making the leucine zipper motif important in many cellular processes.

Examples[edit | edit source]

Examples of proteins that contain a leucine zipper motif include c-Fos and c-Jun, which form the AP-1 transcription factor complex. Other examples include GCN4, C/EBP and bZIP transcription factors.