... 865871 ê 2005 FEBS An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein Lucia Banci1,2, Ivano Bertini1,2, ... HAH1 and either the second or the fifth soluble domains of ATP7A (MNK2 and MNK5, respectively), in the pres-ence of copper(I). The copper-transfer properties of MNK2 and MNK5are similar, and ... without the poly(His)tag shows that there is no detectable interaction between the tag and the remainder of the protein and that the solu-tion structure of MNK5 is not sensitive to the presence of the...