Abstract
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).
Original language | English |
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Pages (from-to) | 2218-2220 |
Number of pages | 3 |
Journal | Biochemistry |
Volume | 53 |
Issue number | 14 |
DOIs | |
Publication status | Published - Apr 15 2014 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Biochemistry