作者: Xiao Tao , Liang Tong
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摘要: 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 DJ-1 contains α/β-fold that is conserved among members DJ-1/ThiJ/PfpI superfamily. However, also an extra helix C terminus, mediates a novel mode dimerization for proteins. A putative active site identified near dimer interface, and residues Cys-106, His-126, Glu-18 may play important roles in catalysis by this protein. Studies with disease-causing L166P mutant suggest mutation disrupted C-terminal region proteins function only as dimers. Lys Arg residue 130, sumoylation minimal impact on