Interactions between copper-binding sites determine the redox status and conformation of the regulatory N-terminal domain of ATP7B.

@article{Leshane2010InteractionsBC,
  title={Interactions between copper-binding sites determine the redox status and conformation of the regulatory N-terminal domain of ATP7B.},
  author={Erik S Leshane and Ujwal Shinde and Joel M. Walker and Amanda Nell Barry and Ninian J. Blackburn and Martina Ralle and Svetlana Lutsenko},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 9},
  pages={
          6327-36
        }
}
Copper-transporting ATPase ATP7B is essential for human copper homeostasis and normal liver function. ATP7B has six N-terminal metal-binding domains (MBDs) that sense cytosolic copper levels and regulate ATP7B. The mechanism of copper sensing and signal integration from multiple MBDs is poorly understood. We show that MBDs communicate and that this communication determines the oxidation state and conformation of the entire N-terminal domain of ATP7B (N-ATP7B). Mutations of copper-coordinating… CONTINUE READING
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