 Abstract mutations have been found to significantly alter the structural flexibility of two switch domains in MIS, an important target of anti-cancer drug design. These mutations cause the switch domains to become more disordered, leading to decreased stability of the protein and reduced activity. Additionally, these mutations lead to changes in the interactions between the protein and its ligand, GTP, which further destabilizes the protein. By analyzing the effects of these mutations on the protein structure and dynamics, researchers have gained insight into how these mutations may contribute to the development of cancer. This article was authored by Hu Yinbao, Wei Wang, Hebo Sun, and others.