Abstract
The basic leucine zipper motif (bZIP) is a simple DNA-binding domain recognizing consensus sequences through interactions between α-helices and DNA. This α-helical domain consists of an N-terminal DNA-binding basic and C-terminal leucine zipper region forming a coiled-coil. As a transcription factor, bZIPs exhibit a high degree of variance in the DNA binding region. This study applies a knob-socket analysis to characterize the multibody determinants of the variation in specificity between individual bZIP monomers and their respective four-base half-site.
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