Journal
BIOCHEMISTRY
Volume 53, Issue 14, Pages 2218-2220Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi500294h
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Funding
- JSPS, Japan [25249115]
- Platform for Drug Discovery, Informatics, and Structural Life Science (MEXT), Japan
- Grants-in-Aid for Scientific Research [25249115, 14J08172, 25000006, 24000011] Funding Source: KAKEN
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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 angstrom 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).
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