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 |
|---|---|
| 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 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
Cite this
Thermodynamic and structural characterization of the specific binding of Zn(II) to human protein DJ-1. / Tashiro, Shinya; Caaveiro, Jose M.M.; Wu, Chun Xiang; Hoang, Quyen Q.; Tsumoto, Kouhei.
In: Biochemistry, Vol. 53, No. 14, 15.04.2014, p. 2218-2220.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Thermodynamic and structural characterization of the specific binding of Zn(II) to human protein DJ-1
AU - Tashiro, Shinya
AU - Caaveiro, Jose M.M.
AU - Wu, Chun Xiang
AU - Hoang, Quyen Q.
AU - Tsumoto, Kouhei
PY - 2014/4/15
Y1 - 2014/4/15
N2 - 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).
AB - 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).
UR - http://www.scopus.com/inward/record.url?scp=84898894283&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84898894283&partnerID=8YFLogxK
U2 - 10.1021/bi500294h
DO - 10.1021/bi500294h
M3 - Article
C2 - 24697266
AN - SCOPUS:84898894283
VL - 53
SP - 2218
EP - 2220
JO - Biochemistry
JF - Biochemistry
SN - 0006-2960
IS - 14
ER -