Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain.
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Lee SJ, Kim SJ, Kim IK, Ko J, Jeong CS, Kim GH, Park C, Kang SO, Suh PG, Lee HS, Cha SS
Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain.
J Biol Chem. 2003 Nov 7;278(45):44552-9. Epub 2003 Aug 25.
- PubMed ID
- 12939276 [ View in PubMed]
- Abstract
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.