Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain
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- Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain
- Lee, SJ; Kim, SJ; Kim, IK; Ko, J; Jeong, CS; Kim, GH; Park, C; Kang, SO; Suh, Pann-Ghill; Lee, HS; Cha, SS
- ONSET PARKINSONS-DISEASE; UBIQUITIN-PROTEIN LIGASE; YEDU GENE-PRODUCT; MOLECULAR CHAPERONE; ANDROGEN RECEPTOR; TRICORN PROTEASE; ALPHA-SYNUCLEIN; DEGRADATION; SUPPRESSION; DROSOPHILA
- Issue Date
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
- JOURNAL OF BIOLOGICAL CHEMISTRY, v.278, no.45, pp.44552 - 44559
- Human DJ-1 and Escherichia coli Hsp31 belong to ThiJ/PfpI family, whose members contain a conserved domain. DJ-1 is associated with autosomal recessive early onset parkinsonism and Hsp31 is a molecular chaperone. Structural comparisons between DJ-1, Hsp31, and an Archaea protease, a member of ThiJ/PfpI family, lead to the identification of the chaperone activity of DJ-1 and the proteolytic activity of Hsp31. Moreover, the comparisons provide insights into how the functional diversity is realized in proteins that share an evolutionarily conserved domain. On the basis of the chaperone activity the possible role of DJ-1 in the pathogenesis of Parkinson's disease is discussed.
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