KRAS is an oncogene that is commonly mutated in human cancer, with mutations occurring in around 30% of all tumours ( ). This makes it a significant focus for drug development. However, progress in this area has been limited because there is no apparent binding pocket, and the nucleotide-binding affinity is considerable. At first, the tactics were centred on posttranslational alterations. However, these strategies faced challenges due to the wide range of substances that the enzymes involved may act upon. In 2013, Kevan Shokat made a significant discovery by devising a technique to target the mutant form of KRASG12C by covalent bonding specifically. This method involved adopting a cysteine-based tethering strategy, which led to the identification of a hidden binding pocket in the switch II domain. The study shows that KRASG12C may be selectively targeted by small compounds that specifically attach to its GDP-bound conformation, thereby offering a novel treatment strategy. Five distinct KRASG12C inhibitors are being tested in clinical trials, namely AMG-510 and MRTX849, which are now in Phase II investigations ).