Journal
FEBS LETTERS
Volume 549, Issue 1-3, Pages 171-175Publisher
WILEY
DOI: 10.1016/S0014-5793(03)00764-6
Keywords
crystal structure; breast cancer; Parkinson's disease; male fertility; protein inhibitor of activated STAT; androgen receptor
Funding
- NCI NIH HHS [P30 CA016086] Funding Source: Medline
- NIGMS NIH HHS [GM59791] Funding Source: Medline
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DJ-1 is a protein involved in multiple physiological processes, including cancer, Parkinson's disease, and male fertility. It is unknown how DJ-1 functions in the apparently different systems. The crystal structure of DJ-1 at 1.6 Angstrom resolution shows that DJ-1 is a helix-strand-helix sandwich and forms a dimer. The DJ-1 structure is similar to the members of the intracellular protease PfpI family. However, the catalytic triad of Cys-His-Glu is not strictly conserved in DJ-1, implying that DJ-1 has a different catalytic mechanism if it acts as a protease or DJ-1 serves as a regulatory protein in the physiological processes. The structure shows that Leu166 positions in the middle of a helix and thus predicts that the L166P mutation will bend the helix and impact the dimerization of DJ-1. As a result, the conformational changes may diminish the DJ-1 binding with its partner, leading to the familial Parkinson's disease caused by the single L166P mutation. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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