In silico structure modeling and analysis of basic leucine zipper-domain containing proteins in Dictyostelium discoideum

Basic leucine zipper domain containing proteins (bZIP) are transcription factors and play crucial role in cellular and developmental regulation. Dictyostelium discoideum has 19 bZIP proteins whose structural and functional analysis is still under investigation. To understand the nature and functionality, we investigated physio-chemical properties and secondary structure of these proteins that revealed the presence of polyQ and polyN runs and a leucine zipper domain. Three-dimensional structures developed by homology modeling showed that proteins have a stable coiled coil and other low complexity regions. The results presented here may help understand the role and working mechanism of these proteins in D. discoideum.