Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease.
Article Details
- CitationCopy to clipboard
Tao X, Tong L
Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease.
J Biol Chem. 2003 Aug 15;278(33):31372-9. Epub 2003 May 21.
- PubMed ID
- 12761214 [ View in PubMed]
- Abstract
We report the crystal structure at 1.8-A resolution of human DJ-1, which has been linked to early onset Parkinson's disease. The monomer of DJ-1 contains the alpha/beta-fold that is conserved among members of the DJ-1/ThiJ/PfpI superfamily. However, the structure also contains an extra helix at the C terminus, which mediates a novel mode of dimerization for the DJ-1 proteins. A putative active site has been identified near the dimer interface, and the residues Cys-106, His-126, and Glu-18 may play important roles in the catalysis by this protein. Studies with the disease-causing L166P mutant suggest that the mutation has disrupted the C-terminal region and the dimerization of the protein. The DJ-1 proteins may function only as dimers. The Lys to Arg mutation at residue 130, the site of sumoylation of DJ-1, has minimal impact on the structure of the protein.