The structure of KRASG12C bound to divarasib highlights features of potent switch-II pocket engagement
Micah C Fernando, Gregory B Craven, Kevan M Shokat · 2025
Read The structure of KRASG12C bound to divarasib highlights features of potent switch-II pocket engagement by Micah C Fernando, Gregory B Craven, Kevan M Shokat (2025) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-12101598.txt.
Description
Fernando, Craven, and Shokat report the crystal structure of a cancer protein bound to a potent new drug. KRAS is the most mutated cancer gene in humans. A change at codon 12 swaps in a cysteine and locks the protein on. Two approved drugs already target that mutant form. A newer agent, divarasib, shows stronger responses in trials. It grips its target tightly and selectively, but its binding shape was unpublished.
The team solved the structure at high resolution. It shows how divarasib engages a pocket called switch-II. Details of the fit explain the drug's punch. The picture can guide the next round of KRAS drug design.
Catalog record
| CREATOR | Micah C Fernando, Gregory B Craven, Kevan M Shokat |
|---|---|
| YEAR | 2025 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 19 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |