The KRAS G12C mutation produces a temporary structural change in the KRAS protein that allows certain drugs to bind, a feature not present in the normal version of the protein.
Not yet evaluated
No evidence has been gathered for this claim yet.
Not medical advice. For informational purposes only. Always consult a healthcare professional.
The KRAS G12C mutation produces a temporary structural change in the KRAS protein that allows certain drugs to bind, a feature not present in the normal version of the protein.
See the technical phrasing
The KRAS G12C mutation creates a transient, druggable allosteric pocket that is absent in the wild-type KRAS protein.
The mutation replaces a normal amino acid with cysteine at position 12, which forces the protein into a rigid shape that creates a hidden pocket near the active site. This pocket only appears briefly during normal protein movement and can be grabbed by drugs that bind to the cysteine. Once bound, the drug pushes on a water molecule that connects to other parts of the protein, causing a chain reaction that twists a key loop and blocks signals that tell cells to grow.
What the research says
Supports
3 studies
Study: Disulfide tethering reveals cryptic pockets in oncogenic KRAS
This study provides evidence supporting the claim.
Contradicts
0 studies
Score breakdown, mechanism chain, raw evidence, ideal studies needed & 3 supporting studies