1.1	Class: Basic leucine zipper factors (bZIP)
Description:	TRANSFAC® class description C0008: A DNA-binding basic region is followed by a leucine zipper. The leucine zipper consists of repeated leucine residues at every seventh position and mediates protein dimerization as a prerequisite for DNA-binding. The leucines are directed towards one side of an alpha-helix. The leucine side chains of two polypeptides are thought to interdigitate upon dimerization (knobs-into-holes model). The leucine zipper dictates dimerization specificity. Upon DNA-binding of the dimer, the basic regions adopt alpha-helical conformation as well. Possibly, a sharp angulation point separates two alpha-helices of the subregions A and B leading to the scissors grip model for the bZIP-DNA complex. The DNA is contacted through the major groove over a whole turn.
Aligned domain sequences:	Alignment of bZIP domains Download fasta file (bZIP domains; ZIP only proteins are not included)
Logo plot:
Dimerization matrix:	Matrix of genus and species dimers (download xls)