Kinase suppressor of Ras-1 (KSR1) is a conserved component of the Ras pathway that acts as a molecular scaffold to promote signal transmission from Raf-1 to MEK and MAPK. All KSR-1 proteins contain a conserved cysteinerich C1 domain, and studies have implicated this domain in the regulation of KSR-1 sub cellular localization and function. In this study an evaluation on binding affinity of coumarin and anthraquinone derivatives on crystal structure of C1 domain of kinase suppressor of RAS was carried out using docking studies. Study showed the occupancy and importance of certain functional groups at the anthraquinone and coumarin nucleus responsible for its potential affinity in binding. These ligands can serve as a lead moiety in developing a targeted drug against the kinase suppressor of ras-1 to interrupt MAPK signaling in neoplasia.
