热动力学和结构特征分析表明 Zn(II)与人蛋白 DJ-1 的特异性结合。
Thermodynamic and structural characterization of the specific binding of Zn(II) to human protein DJ-1.
机构信息
Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo , Kashiwa 277-8562, Japan.
出版信息
Biochemistry. 2014 Apr 15;53(14):2218-20. doi: 10.1021/bi500294h. Epub 2014 Apr 3.
Mutations of DJ-1 cause familial Parkinson's disease (PD), although the role of DJ-1 in PD remains unresolved. Very recent reports have shown that DJ-1 interacts with copper ions. This evidence opens new avenues to understanding the function of DJ-1 and its role in PD. Herein, we report that Zn(II) binds to DJ-1 with great selectivity among the other metals examined: Mn(II), Fe(II), Co(II), Ni(II), and Cu(II). High-resolution X-ray crystallography (1.18 Å resolution) shows Zn(II) is coordinated to the protein by the key residues Cys106 and Glu18. These results suggest that DJ-1 may be regulated and/or stabilized by Zn(II).
DJ-1 突变导致家族性帕金森病（PD），尽管 DJ-1 在 PD 中的作用仍未解决。最近的报道表明 DJ-1 与铜离子相互作用。这一证据为理解 DJ-1 的功能及其在 PD 中的作用开辟了新的途径。在此，我们报告 Zn(II)在我们研究的其他金属中（Mn(II)、Fe(II)、Co(II)、Ni(II)和 Cu(II)）对 DJ-1 具有很高的选择性结合。高分辨率 X 射线晶体学（1.18 Å 分辨率）显示 Zn(II)通过关键残基 Cys106 和 Glu18 与蛋白质配位。这些结果表明 DJ-1 可能受 Zn(II)的调节和/或稳定。
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