Ordering the Disordered Proteins

Intrinsically disordered proteins (IDPs) are key components of regulatory networks that dictate various aspects of cellular decision-making. They are over-represented in major disease pathways, and are considered novel albeit currently difficult drug targets. IDPs are biologically active proteins without stable structure. Therefore designing drugs based on 3D structure of those proteins is a complex task. It has already been shown that there is a role of electrostatic interactions in promoting efficient coupled binding and folding for facile specific recognition in IDPs in protein-protein interactions. In the present work we investigated the role of IDPs electrostatic in protein-DNA interactions. The results show that the disordered regions are involved in DNA binding. We suggest that electrostatic should be taken into account to a greater extent while designing drugs for IDPs targets.