1j42

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[[Image:1j42.gif|left|200px]]
[[Image:1j42.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j42 OCA], [http://www.ebi.ac.uk/pdbsum/1j42 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j42 RCSB]</span>
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'''Crystal Structure of Human DJ-1'''
'''Crystal Structure of Human DJ-1'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Cha, S S.]]
[[Category: Cha, S S.]]
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[[Category: parkinson's disease]]
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[[Category: Parkinson's disease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:46:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:28:33 2008''
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Revision as of 17:46, 2 May 2008

Image:1j42.gif

Template:STRUCTURE 1j42

Crystal Structure of Human DJ-1


Overview

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.

About this Structure

1J42 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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 PG, Lee HS, Cha SS, J Biol Chem. 2003 Nov 7;278(45):44552-9. Epub 2003 Aug 25. PMID:12939276 Page seeded by OCA on Fri May 2 20:46:58 2008

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