Malonate in the nucleotide-binding site traps human AKAP18γ/δ in a novel conformational state.

@article{BjerregaardAndersen2016MalonateIT,
  title={Malonate in the nucleotide-binding site traps human AKAP18$\gamma$/$\delta$ in a novel conformational state.},
  author={Kaare Bjerregaard-Andersen and Ellen {\O}stensen and John D. Scott and Kjetil Task{\'e}n and Jens Preben Morth},
  journal={Acta crystallographica. Section F, Structural biology communications},
  year={2016},
  volume={72 Pt 8},
  pages={
          591-7
        }
}
A-kinase anchoring proteins (AKAPs) are a family of proteins that provide spatiotemporal resolution of protein kinase A (PKA) phosphorylation. In the myocardium, PKA and AKAP18γ/δ are found in complex with sarcoendoplasmic reticulum Ca(2+)-ATPase 2 (SERCA2) and phospholamban (PLB). This macromolecular complex provides a means by which anchored PKA can dynamically regulate cytoplasmic Ca(2+) release and re-uptake. For this reason, AKAP18γ/δ presents an interesting drug target with therapeutic… 

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