1j42
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(New page: 200px<br /> <applet load="1j42" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j42, resolution 2.50Å" /> '''Crystal Structure o...)
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Revision as of 15:30, 12 November 2007
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Crystal Structure of Human DJ-1
Contents |
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.
Disease
Known diseases associated with this structure: Amyotrophic lateral sclerosis-Parkinsonism/dementia complex 2 OMIM:[602533], Parkinson disease 7, autosomal recessive early-onset OMIM:[602533]
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
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