The Aurora kinases play essential roles in mitosis and have received attention as targets for drug-development. Aurora-A represents a promising target for development of anticancer therapeutics; however whilst potent and selective active site inhibitors have been identified, these have yet to be approved for therapeutic use. Such compounds might be expected to have a narrow therapeutic window because Aurora-A has many roles, including a critical function in bipolar mitotic spindle assembly. Aurora-A is an incomplete kinase; its localization and activation are regulated through protein-protein interactions (PPIs). Targeting these PPI interfaces may represent an alternative approach to ATP-competitive inhibitors. One candidate PPI is the N-Myc/Aurora-A interaction. MYCN (the gene that encodes for the N-Myc protein) was discovered through its association with neuroblastoma, a cancer of the nervous system that affects children. Elevated levels of N-Myc have also been observed in several other cancers. In 2016, Richards et al. published an X-ray co-crystal structure of Aurora-A in complex with an intrinsically disordered region of N-MYC (residues 28-89); although residues 28-60 were not observed in the structure, residues 61-89 of N-Myc were found to undergo a disorder to order transition to interact in an α-helical conformation with the cleft between the Aurora-A N-and C-lobes formed by the αB-/αC-helices, the A-loop, and the αG-helix (Fig. ).