Oncogenic and RASopathy-Associated K-RAS Mutations Relieve Membrane-Dependent Occlusion of the Effector-Binding Site

Mazhab-Jafari M, et al., 112(21):6625-30, Proc Natl Acad Sci U S A, 2015

Described herein are the NMR-derived models pertaining to plausible interactions between Kirsten rat sarcoma viral oncogene homolog 4B (K-RAS4B) and the lipid membrane biolayer. The report also evaluates how theose interactions could affect oncogenic and RASopathy-associated K-RAS mutations. Binding of K-RAS4B to Anti-GST antibody-coated biosensor immobilized ARAF-RBD was studied by Bio-Layer Interferometry (BLI) using a Pall ForteBio Octet RED96 instrument. Overall results suggest that the tendency of K-RAS4B to interact with the membrane in a way that occludes its effector binding site may reveal a new therapeutic target.

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