Kinase Suppressor of Ras (KSR) is a molecular scaffold that interacts with the 
core kinase components of the ERK cascade, Raf, MEK, ERK to provide spatial and 
temporal regulation of Ras-dependent ERK cascade signaling. Interruption of this 
mechanism can have a high influence in inhibiting the downstream signaling of 
the mutated tyrosine kinase receptor kinase upon ligand binding. Still none of 
the studies targeted to prevent the binding of Raf, MEK binding on kinase 
suppressor of RAS. In that perspective the cysteine rich C1 domain of scaffold 
proteins kinase suppressor of Ras-1 was targeted rather than its ATP binding 
site with small ligand molecules like flavones and anthocyanidins and analyzed 
through insilico docking studies. The binding energy evaluation shows the 
importance of hydroxyl groups at various positions on the flavone and 
anthocyanidin nucleus. Over all binding interaction shows these ligands occupied 
the potential sites of cysteine rich C1 domain of scaffold protein KSR.