Thermodynamic and structural characterization of the specific binding of Zn(II) to human protein DJ-1

Shinya Tashiro, Jose M M Caaveiro, Chun Xiang Wu, Quyen Hoang, Kouhei Tsumoto

Research output: Contribution to journalArticle

6 Citations (Scopus)

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 languageEnglish
Pages (from-to)2218-2220
Number of pages3
JournalBiochemistry
Volume53
Issue number14
DOIs
StatePublished - Apr 15 2014

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Thermodynamics
Parkinson Disease
X ray crystallography
X Ray Crystallography
Copper
Metals
Ions
Mutation
human PARK7 protein
Proteins

ASJC Scopus subject areas

  • 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; Tsumoto, Kouhei.

In: Biochemistry, Vol. 53, No. 14, 15.04.2014, p. 2218-2220.

Research output: Contribution to journalArticle

Tashiro, Shinya ; Caaveiro, Jose M M ; Wu, Chun Xiang ; Hoang, Quyen ; Tsumoto, Kouhei. / Thermodynamic and structural characterization of the specific binding of Zn(II) to human protein DJ-1. In: Biochemistry. 2014 ; Vol. 53, No. 14. pp. 2218-2220.
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