Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease.
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.
Mesh Terms:
Age of Onset, Amino Acid Sequence, Binding Sites, Catalysis, Crystallography, Dimerization, Humans, Intracellular Signaling Peptides and Proteins, Molecular Sequence Data, Oncogene Proteins, Parkinson Disease, Point Mutation, Protein Structure, Secondary, Protein Structure, Tertiary, SUMO-1 Protein, Sequence Homology, Amino Acid
Age of Onset, Amino Acid Sequence, Binding Sites, Catalysis, Crystallography, Dimerization, Humans, Intracellular Signaling Peptides and Proteins, Molecular Sequence Data, Oncogene Proteins, Parkinson Disease, Point Mutation, Protein Structure, Secondary, Protein Structure, Tertiary, SUMO-1 Protein, Sequence Homology, Amino Acid
J. Biol. Chem.
Date: Aug. 15, 2003
PubMed ID: 12761214
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