An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein
An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein
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DOI：
10.1111/j.1742-4658.2004.04526.x
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发表时间：
2005-02-01
期刊：
影响因子：
5.4
通讯作者：
Rosato, A
中科院分区：
文献类型：
--
作者：
Banci, L;Bertini, I;Rosato, A
利用异核核磁共振在溶液中研究了人类铜（I）伴侣蛋白HAH1与其两个生理伙伴之一——门克斯病蛋白（ATP7A）之间的相互作用。该研究是在铜（I）存在的情况下，通过涉及HAH1以及ATP7A的第二个或第五个可溶性结构域（分别为MNK2和MNK5）的滴定来进行的。MNK2和MNK5的铜转移特性相似，且与先前在酵母同源系统中观察到的特性有显著差异。特别是，在MNK结构域与HAH1之间没有形成稳定的加合物。在核磁共振化学位移的时间尺度上，铜（I）转移反应缓慢，并且平衡明显向铜（I） - MNK2/MNK5的形成方向移动。还报道了之前未有的脱辅基 - 和铜（I） - MNK5的溶液结构。将结果与文献中从其他光谱技术获得的关于HAH1及其伙伴之间相互作用的数据进行比较并展开了讨论。
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 HAM and its partners from other spectroscopic techniques.