Figure 3
From: Studies on the regulatory mechanism of isocitrate dehydrogenase 2 using acetylation mimics
Structural comparison of wild-type mIDH2 and the K256Q mutant. (a) Structural alignment of the wild-type mIDH2 (light blue) and the K256Q mutant (tan) proteins. The two circles show conformational differences between the two structures. The regions that are structurally different in the large domain have been highlighted with different colors (green for wild-type mIDH2 and magenta for the K256Q mutant). (b,c) Enlarged view of large domains from the structural overlay of wild-type mIDH2 and the K256Q mutant for subunits A (b) and B (c), respectively. Red arrows represent the structural differences in K256Q compared to the wild-type structure. Mg2+ ions are represented by green spheres, and isocitrate molecules are represented by purple sticks and yellow sticks in wild-type mIDH2 and the K256Q mutant, respectively.
