Modeling receptor flexibility in the structure-based design of KRASG12C inhibitors.

Abstract excerpt

KRAS has long been referred to as an 'undruggable' target due to its high affinity for its cognate ligands (GDP and GTP) and its lack of readily exploited allosteric binding pockets. Recent progress in the development of covalent inhibitors of KRASG12C has revealed that occupancy of an allosteric binding site located between the α3-helix and switch-II loop of KRASG12C-sometimes referred to as the 'switch-II...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Guanosine Triphosphate
• Share to Ligands
• Share to Mutation