What question did this study set out to answer?

The study aims to explore the distinct structural and functional differences between KRAS G12C and G12D mutants and their implications in oncogenesis.

March 7, 2026Cancer Research

Abstract A047: KRAS G12C and G12D mutants exhibit distinct conformational flexibility in the helix 3–switch 2 pocket that drives differential protein function

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The study aims to explore the distinct structural and functional differences between KRAS G12C and G12D mutants and their implications in oncogenesis.
Utilized NMR solution structures to analyze conformational differences in KRAS mutants.
Conducted Bioluminescence Resonance Energy Transfer (BRET) assays to assess binding affinities.
Performed 31P NMR analyses to investigate the effects of the pan-KRAS inhibitor BBO-11534.
KRAS G12D exhibits a larger SW2-pocket compared to KRAS G12C, influencing effector binding affinity.
BBO-11534 shifts conformational states in KRAS G12D more effectively than in G12C.
Binding assessments reveal KRAS G12D has significantly higher affinity for p110α than both G12C and wild-type.

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Implication

NMR analysis reveals differentiated protein functions driven by conformational variations in KRAS mutants, indicating potential therapeutic targets.

Cite This Study

Sharma et al. (2026) studied this question.

synapsesocial.com/papers/69abc1b45af8044f7a4ea94e https://doi.org/10.1158/1538-7445.rasoncother26-a047

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Implication

NMR analysis reveals differentiated protein functions driven by conformational variations in KRAS mutants, indicating potential therapeutic targets.

Abstract A047: KRAS G12C and G12D mutants exhibit distinct conformational flexibility in the helix 3–switch 2 pocket that drives differential protein function

Key Points

Discussion

Implication

Cite This Study

Abstract A047: KRAS G12C and G12D mutants exhibit distinct conformational flexibility in the helix 3–switch 2 pocket that drives differential protein function

Key Points

Discussion

Implication

Cite This Study

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