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Background: Oncoprotein 18 (Op18) is a proliferation-related cytosolic phosphoprotein which is induced in normal lymphocytes following mitogenic stimulation. Studies of Op18 are of particular interest because of the proposed role it plays in signal transduction and because of its occurrence in markedly increased amounts in acute leukemia cells (1). Oncoprotein 18 has been independently identified due to its increased phosphorylation in response to external signals and its up-regulated expression in acute leukemia. Findings suggest that Op18 may be a physiological substrate for several members of the cdc2 kinase family during both the S-phase and the mitotic phase of the cell cycle (2). Also, findings show that Op18 by itself can fold into a flexible and extended alpha-helix, which is in equilibrium with a less ordered structure. In complex with tubulin, however, all except the last seven C-terminal residues of Op18 are tightly bound to tubulin. Studies suggest results suggest that besides sequestering tubulin, the structural features of Op18 enable the protein specifically to recognize microtubule ends to trigger catastrophes (3).