A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.

@article{Banci2005ANS,
  title={A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.},
  author={Lucia Banci and Ivano Bertini and Francesca Cantini and Christos T. Chasapis and Nick Hadjiliadis and Antonio Rosato},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 46},
  pages={38259-63}
}
ATP7A is a P-type ATPase involved in copper(I) homeostasis in humans. It possesses a long N-terminal tail protruding into the cytosol and containing six copper(I)-binding domains, which are individually folded and capable of binding one copper(I) ion. ATP7A receives copper from a soluble protein, the metallochaperone HAH1. The exact role and interplay of the six soluble domains is still quite unclear, as it has been extensively demonstrated that they are strongly redundant with respect to… CONTINUE READING

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