Abstract
The primary structure of the different PKC subspecies contains an ATP-binding sequence in the catalytic domain. The α, β, and γ isoforms contain an additional ATP-binding consensus sequence whose significance remains unknown. To explain this function and also to prepare new specific PKC inhibitors, bis-ATP molecules have been synthesized. The variation of the mutual position of the ATP mimics is conditioned by the choice of the included spacer. The products generally have an increased inhibitor potency towards PKC, PKA and HL60 tyrosin kinase. The inhibition is always competitive towards ATP but does not allow the conclusion that a simultaneous interaction occurs at both ATP-binding sites.
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