Interaction of cAMP derivatives with the 'stable' cAMP-binding site in the cAMP-dependent protein kinase type I.

@article{Wit1982InteractionOC,
  title={Interaction of cAMP derivatives with the 'stable' cAMP-binding site in the cAMP-dependent protein kinase type I.},
  author={R R J C de Wit and J. O. Hoppe and Wojciech J. Stec and Janina Baraniak and Bernd Jastorff},
  journal={European journal of biochemistry},
  year={1982},
  volume={122 1},
  pages={95-9}
}
cAMP binding to the 'stable' cAMP-binding sites in the regulatory subunit of the cAMP-dependent protein kinase type I was investigated using a set of 18 selected derivatives. All the tested analogues were competitive with [3H]cAMP and inhibitor constants from 12 nM to 20 microM with the free regulatory subunit were determined. The cAMP molecule seemed to be bound by these specific hydrogen bonds to the 5' and 3' oxygen, the 2' hydroxyl, and an ion pair interaction between the negative charge in… CONTINUE READING

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