Molecular basis of AKAP specificity for PKA regulatory subunits.

@article{Gold2006MolecularBO,
  title={Molecular basis of AKAP specificity for PKA regulatory subunits.},
  author={Matthew G Gold and Birgitte Lygren and Pawel Dokurno and Naoto Hoshi and George McConnachie and Kjetil Task{\'e}n and Cathrine Rein Carlson and John D Scott and David Barford},
  journal={Molecular cell},
  year={2006},
  volume={24 3},
  pages={383-95}
}
Localization of cyclic AMP (cAMP)-dependent protein kinase (PKA) by A kinase-anchoring proteins (AKAPs) restricts the action of this broad specificity kinase. The high-resolution crystal structures of the docking and dimerization (D/D) domain of the RIIalpha regulatory subunit of PKA both in the apo state and in complex with the high-affinity anchoring peptide AKAP-IS explain the molecular basis for AKAP-regulatory subunit recognition. AKAP-IS folds into an amphipathic alpha helix that engages… CONTINUE READING

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