We also observed in the energy minimum structure of the complex, that Pro531 TACC3 exhibits a C γ -exo-pucker conformation, which likely facilitates deeper insertion of the side-chain into a hydrophobic pocket on Aurora-A (Leu130 Aurora-A , Ile134 Aurora-A and Glu135 Aurora-A Fig. , Fig. ). The exo-pucker conformation at the proline residue allows a peptidyl-prolyl trans-amide bond of the preceding residue, which favors the accommodation and propagation of the TACC3 backbone chain across the surface of Aurora-A.