Structural motif seen in many DNA-binding proteins in which two helices from separate proteins are joined together in a coiled-coil, forming a protein dimer.
A structural motif characteristic of DNA-binding proteins consisting of a protein dimer formed by two interacting a helices from separate proteins.
A motif found in certain proteins in which Leu residues are evenly spaced through an a-helical region, such that they would end up on the same face of the helix. Dimers can form between two such proteins. The Leu zipper is important in the function of transcription factors such as Fos and Jun and related proteins.
Protein motif which binds DNA in which 4-5 Leucines are found at 7 amino acid intervals. This motif is present typically in transcription factors and other proteins that bind DNA.
Configuration of a DNA-binding protein in which leucine residues on two protein alpha-helices interdigitate in zipper fashion to stabilize the protein.
A molecular motif in which a set of four or five consecutive leucine residues is repeated every seven amino acids in the primary sequence.
Common structural motif in some dimeric eukaryotic transcription factors characterized by a C-terminal coiled-coil dimerization domain and N-terminal DNA-binding domain. ( Figure 10-43)
The leucine zipper is a type of structural motif found in parallel coiled coils. It is a common dimerization domain found in some proteins involved in regulating gene expression.
