bZip Dimers : 'Genetic Chopsticks'

3D Model

MafB is a well-known transcription factor (TF) that forms into a ‘Basic Leucine Zipper’ (bZip)… and is colloquially thought of as the ***’chop-stick’ *** of molecular bioscience. It’s physique is derived from two alpha helical structures which cross over each other and settle down into opposite grooves of DNA - effectively grasping it!

MafB can either form a homodimer with itself (symmetrical zip), or a heterodimer with another compatible helical protein (asymmetrical). An asymmetric candidate for a heterodimeric arrangement is the transcription factor c-Fos. Both arrangements will yield a comparatively unique bonding pattern and thus, a different comformation of the resulting TF/DNA complex! This gives rise to some very interesting biochemistry in terms of how this TF family can regulate our genome through combinatorial versatility.

What exactly is responsible for the diversity and function of these grand biological utensils and how can we modify it … let’s now look at the puzzle pieces :)