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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain

Cited 137 times inthomson ciCited 131 times inthomson ci
Title
Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain
Author
Lee, SJKim, SJKim, IKKo, JJeong, CSKim, GHPark, CKang, SOSuh, Pann-GhillLee, HSCha, SS
Keywords
ONSET PARKINSONS-DISEASE; UBIQUITIN-PROTEIN LIGASE; YEDU GENE-PRODUCT; MOLECULAR CHAPERONE; ANDROGEN RECEPTOR; TRICORN PROTEASE; ALPHA-SYNUCLEIN; DEGRADATION; SUPPRESSION; DROSOPHILA
Issue Date
200311
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, v.278, no.45, pp.44552 - 44559
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.
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DOI
http://dx.doi.org/10.1074/jbc.M304517200
ISSN
0021-9258
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