- 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...
Expand abstract - Publication status:
- Published
- 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
- Language:
- English
- Keywords:
- Copyright date:
- 2013
Journal article
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.
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