Fig. 3

Cancer-related MxA mutations in G domain. a L95 is deeply buried in a hydrophobic cave. b P96 leads the direction of Switch I, which embraces guanine triphosphate nucleotide. c S134 is located on the surface of the G domain. d P218 sits at the end of β-strand 4 (β4 _G ). e V263 is loosely enwrapped by neighboring hydrophobic residues. f R310 is exposed to the solvent and takes two side chain conformations, whereas K326N interacts with vicinal residues. All cancer-related mutations are shown as the original (i.e., non-mutated) residues, and the post-mutation residues are included in the labels, as L(original)95P(post-mutation), and so on. This scheme is also applied to all of the following figures