About Basic leucine zipper factors (bZIP)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.
More informationSpecies within this Class: 41
Genera within this Class: 53
LOGO plot of the DNA binding domain
FASTA file of the LogoPlot
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DNA binding domain |
Whole protein |
| FASTA |
FASTA file |
FASTA file |
Phylogenetic tree Mammalia
(slim selection)
To generate these trees, only the TFs were taken from a selected group of mammalian species. As standard, the corresponding human, cow, mouse and Monodelphis TFs were taken if available; occasionally, either species was to replaced or had to be omitted without replacement.
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