The interaction between the human copper(I) chaperone, HAH1, and one of its two physiological partners, the Menkes disease protein (ATP7A), was investigated in solution using heteronuclear NMR. The study was carried out through titrations involving HAH1 and either the second or the fifth soluble domains of ATP7A (MNK2 and MNK5, respectively), in the presence of copper(I). The copper-transfer properties of MNK2 and MNK5 are similar, and differ significantly from those previously observed for the yeast homologous system. In particular, no stable adduct is formed between either of the MNK domains and HAH1. The copper(I) transfer reaction is slow on the time scale of the NMR chemical shift, and the equilibrium is significantly shifted towards the formation of copper(I)-MNK2/MNK5. The solution structures of both apo- and copper(I)-MNK5, which were not available, are also reported. The results are discussed in comparison with the data available in the literature for the interaction between HAH1 and its partners from other spectroscopic techniques.

An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein / L.Banci; I.Bertini; S.Ciofi-Baffoni; C.T.Chasapis; N.Hadjiliadis; A.Rosato. - In: THE FEBS JOURNAL. - ISSN 1742-464X. - STAMPA. - 272:(2005), pp. 865-871. [10.1111/j.1742-4658.2004.04526.x]

An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein

BANCI, LUCIA;BERTINI, IVANO;CIOFI BAFFONI, SIMONE;ROSATO, ANTONIO
2005

Abstract

The interaction between the human copper(I) chaperone, HAH1, and one of its two physiological partners, the Menkes disease protein (ATP7A), was investigated in solution using heteronuclear NMR. The study was carried out through titrations involving HAH1 and either the second or the fifth soluble domains of ATP7A (MNK2 and MNK5, respectively), in the presence of copper(I). The copper-transfer properties of MNK2 and MNK5 are similar, and differ significantly from those previously observed for the yeast homologous system. In particular, no stable adduct is formed between either of the MNK domains and HAH1. The copper(I) transfer reaction is slow on the time scale of the NMR chemical shift, and the equilibrium is significantly shifted towards the formation of copper(I)-MNK2/MNK5. The solution structures of both apo- and copper(I)-MNK5, which were not available, are also reported. The results are discussed in comparison with the data available in the literature for the interaction between HAH1 and its partners from other spectroscopic techniques.
2005
272
865
871
L.Banci; I.Bertini; S.Ciofi-Baffoni; C.T.Chasapis; N.Hadjiliadis; A.Rosato
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/320275
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