Abstract
We simulated the docking of two teleocidin congeners to the cys2 domain structure observed in the crystalline complex of protein kinase Cδ with phorbol-13-acetate. The most stable docking models were searched for two conformers of (-)-indolactam-V ((-)-IL-V), twist and sofa form, and for (-)-benzolactam-V ((-)-BL-V8) by using an automatic docking method, ADAM, which can cover all possible binding modes and conformations. The twist form of (-)-IL-V and (-)-BL-V8 molecules fitted well into the same cavity as phorbol-13-acetate. Of the three functional groups hydrogen-bonding to the protein, two hydrogen-bonded with protein atoms in common with phorbol-13-acetate, but the third one hydrogen-bonded with a different protein atom from that in the case of phorbol-13-acetate.
