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Lookup NU author(s): Dr Dr MD Harrison Harrison
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The Menkes ATPase (MNK) has an essential role in the translocation of copper across cellular membranes. In a complementary manner, the intracellular concentration of copper regulates the activity and cellular location of the ATPase through its six homologous amino-terminal domains. The roles of the six amino-terminal domains in the activation and cellular trafficking processes are unknown. Understanding the role of these domains relies on the development of an understanding of their metal-binding properties and structural properties. The second conserved sub-domain of MNK was over-expressed, purified and its copper-binding properties characterised. Reconstitution studies demonstrate that copper binds to MNKr2 as Cu(I) with a stoichiometry of one copper per domain. This is the first direct evidence of copper-binding to the MNK amino-terminal repeats. Circular dichroism studies suggest that the binding or loss of copper to MNKr2 does not cause substantial changes to the secondary structure of the protein.
Author(s): Harrison MD, Meier S, Dameron CT
Publication type: Article
Publication status: Published
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
Year: 1999
Volume: 1453
Issue: 1
Pages: 254-260
Print publication date: 24/02/1999
ISSN (print): 0006-3002
Publisher: Elsevier
URL: http://dx.doi.org/10.1016/S0925-4439(98)00110-0
DOI: 10.1016/S0925-4439(98)00110-0
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