Skip to main content
. 2023 Aug 18;14:1223433. doi: 10.3389/fimmu.2023.1223433

Figure 1.

Figure 1

(A) An alignment of the carboxy terminus of the three RAS isoforms is shown. The RAS subtypes are highly conserved (~90%) with respect to the entire amino terminal GTPase domain (amino acids 1–166), which contains the GTP-GDP binding site and the interaction site of the effector protein; however, the carboxy terminal part differs and is called the hypervariable zone. (B) Percentages of KRAS mutations in codon 12 and NRAS mutations in codon 61 by tissue type for common cancers. (C) The canonical nature of RAS is characteristic of a small GTPase that usually circulates between the GTP-bound active state and GDP-bound inactive state, which is partly promoted by the GTP hydrolysis-stimulating GTPase activation protein (GAP). However, when the RAS protein is mutated, impaired GAP stimulation promotes the formation of a persistently GTP-bound RAS. (D) An overview of the general biochemical destruction of hydrolysis and guanine exchange after mutation of codon 12 or 61.