The small guanine nucleotide binding protein Ras is involved in cellular signal transduction and cell proliferation. Conformation states of p21ras
are associated with interaction of effectors regulating the signal transduction and cell proliferation. From NMR studies it is revealed that state 2 is an active form of GTP bound Ras with high affinity to Raf-Kinase, while state 1 is shown to be a
conformation similar to GDP bound state. Stabilization of this latter state has an importance in development of antitumor strategies by regulating the interaction of effectors with active and inactive states of nucleotide bound Ras. Here ubiquitous
Ras*GTP properties and its interaction with effectors were investigated in order to down regulate the signal transduction from the following strategies
A) Switching mechanism,
B) Acceleration of GTP hydrolysis by metal macrocycles
C) Emulating GTPase Activating Protein mimics
D) Photo Dynamic Therapeutic Applications on Nucleotide dissociation.