Aurora kinases are serine/threonine kinases that are essential for cell proliferation. The enzyme helps the dividing cell share its genetic materials with its daughter cells. More specifically, Aurora kinases play a crucial role in cellular division by controlling chromatid segregation. Defects in this segregation can cause genetic instability, a condition which is highly associated with tumorigenesis (Bolanos-Garcia, 2005). Three Aurora kinases have been identified in mammalian cells to date. Besides being implicated as mitotic regulators, these three members of the mammalian family have generated significant interest in the cancer research field due to their elevated expression profiles in many human cancers (Giet & Prigent, 1999). The human Aurora kinases present a similar domain organization, with a N-terminal domain of 39 to 129 residues in length, a protein kinase domain and a short C-terminal domain containing 15 to 20 residues. The N-terminal domain of three proteins share low sequence conservation, which determines selectivity during protein-protein interactions (Bolanos-Garcia, 2005).