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

Puno, M. Rhyan; Patel, Nisha A.; Møller, Simon Geir; Robinson, Carol V.; Moody, Peter C. E.; Odell, Mark;
  • Publisher: Figshare
  • Related identifiers: doi: 10.1021/ja406010m.s002, doi: 10.1021/ja406010m.s001
  • Subject: Molecular Biology | homodimer interactions | DJ | SOD | oxidation state | biscysteinate site | Genetics | Homodimer Interface | Mutational Inactivation | Biophysics | subfemtomolar dissociation | Neuroscience | Medicine | copper cofactor | cysteine residues | Cu | Cell Biology | Biochemistry | metal coordination | crystal structure | Biscysteinate Metal Binding Site | metal ion | crystallo validates | copper binding
    • FOR: 29999 Physical Sciences not elsewhere classified | 69999 Biological Sciences not elsewhere classified | 39999 Chemical Sciences not elsewhere classified

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 characte... View more
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