The KRAS G12D mutation in pancreatic cancer does not create the specific structural site that drugs targeting the G12C mutation are designed to bind.
Strongly supported
Multiple high-quality studies back this claim.
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The KRAS G12D mutation in pancreatic cancer does not create the specific structural site that drugs targeting the G12C mutation are designed to bind.
See the technical phrasing
The KRAS G12D mutation, which is prevalent in pancreatic cancer, does not generate an allosteric pocket that is targeted by inhibitors designed for the G12C mutation.
The G12D mutation changes the shape of the KRAS protein near its active site, creating a unique pocket that only certain drugs can fit into. Drugs designed for the G12C mutation cannot bind to this different shape, so they have no effect. A different drug must be made to lock the G12D version in an inactive state by fitting precisely into its own unique pocket.
What the research says
Supports
3 studies
Study: Abstract 4569: D3S-003, an orally bioavailable potent and selective dual-state inhibitor targeting both GDP- and GTP-bound KRAS G12D
This study provides evidence supporting the claim.
Contradicts
0 studies
Score breakdown, mechanism chain, raw evidence, ideal studies needed & 3 supporting studies