Leucine zipper as a fine tuner for the DNA binding; Revisited with molecular dynamics simulation of the Fos-Jun bZIP complex

Leucine zipper dynamically tunes the degree of bifurcation of the DNA binding segments in the basic region of the Foe-Jun bZIP complex. Molecular dynamics simulation indicated that site-specific mutagenesis of conserved leucine residues inside the leucine zipper domain caused the change of dynamic behavior of the basic region, and efficient DNA binding occurs only within a certain range of distance between the two DNA binding segments in the basic region. Distribution of alpha-helices in the hinge region is also suggested to influence the bifurcation of the DNA binding segments.