1J42
Crystal Structure of Human DJ-1
Summary for 1J42
| Entry DOI | 10.2210/pdb1j42/pdb |
| Descriptor | RNA-binding protein regulatory subunit (2 entities in total) |
| Functional Keywords | parkinson's disease, rna binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane ; Lipid-anchor : Q99497 |
| Total number of polymer chains | 1 |
| Total formula weight | 19873.02 |
| Authors | Cha, S.S. (deposition date: 2003-02-26, release date: 2004-02-03, Last modification date: 2023-12-27) |
| Primary citation | Lee, S.J.,Kim, S.J.,Kim, I.K.,Ko, J.,Jeong, C.S.,Kim, G.H.,Park, C.,Kang, S.O.,Suh, P.G.,Lee, H.S.,Cha, S.S. Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain. J.Biol.Chem., 278:44552-44559, 2003 Cited by 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. PubMed: 12939276DOI: 10.1074/jbc.M304517200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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