KRAS and neoplasm: MRTX-1133 also inhibits the binding of RAF-RAS binding domain peptides to the active form of KRASG12D with an IC50 of 9 nM, and induces conformational changes in switch I and switch II regions of KRAS protein.254 By interacting with aspartic acid Asp12 and glutamic acid Glu62 in the switch II region of KRAS protein, MRTX-1133 plays an allosteric role, resulting in conformational changes of KRAS protein and inhibition of the KRAS signaling pathway in cells and tumor environments containing KRASG12D mutations, thereby achieving an antitumor effect.