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Structure of Cu(I)-bound DJ-1 reveals a biscysteinate metal binding site at the homodimer interface: insights into mutational inactivation of DJ-1 in Parkinsonism.

Abstract:

The Parkinsonism-associated protein DJ-1 has been suggested to activate the Cu-Zn superoxide dismutase (SOD1) by providing its copper cofactor. The structural and chemical means by which DJ-1 could support this function is unknown. In this study, we characterize the molecular interaction of DJ-1 with Cu(I). Mass spectrometric analysis indicates binding of one Cu(I) ion per DJ-1 homodimer. The crystal structure of DJ-1 bound to Cu(I) confirms metal coordination through a docking accessible bis...

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Publication status:
Published

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Publisher copy:
10.1021/ja406010m

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Journal:
Journal of the American Chemical Society
Volume:
135
Issue:
43
Pages:
15974-15977
Publication date:
2013-10-05
DOI:
EISSN:
1520-5126
ISSN:
0002-7863
URN:
uuid:2d4e7087-0ca6-49eb-bbb2-fc869fc590fe
Source identifiers:
439628
Local pid:
pubs:439628

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