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Comment
. 2003 Aug 5;100(16):9111-3.
doi: 10.1073/pnas.1633722100. Epub 2003 Jul 28.

Crystallizing ideas about Parkinson's disease

Mark R Cookson  1
Affiliations
Comment

Crystallizing ideas about Parkinson's disease

Mark R Cookson. Proc Natl Acad Sci U S A. .
No abstract available

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Figures

Fig. 1.
Fig. 1.
Similarities and differences in structures of different members of the DJ-1 superfamily. (A) Monomers of human DJ-1 and two structural homologues, the P. horikoshii protease PH1704 and the E. coli chaperone Hsp31. Each monomer was redrawn from database coordinates at the Research Collaboratory for Structural Bioinformatics (www.rcsb.org) to give broadly similar orientations for all three molecules. In this view, β-strands (green) are found in the center of the structure, surrounded by α-helixes (magenta). Note the presence of an extra α-helix at the C terminus of DJ-1 compared with PH1704, which strongly affects packing of the protein into a dimer. The larger Hsp31 protein is also organized in a similar fashion with a centralβ-sheet rich region surrounded by helices. Note also that all three proteins have a β-hairpin (oriented at the bottom of these figures), which plays a role in the dimerization of DJ-1. (B) A dimer of DJ-1 compared with a trimer of PH1704. DJ-1 has been crystallized as a dimer, the two monomers represented in blue and red. PH1704 is represented as a trimer to illustrate the relative orientation of the three monomers; the protein is actually hexameric and consists of two units similar to the structure shown forming a closed ring. The red monomer is in approximately the same orientation as the red monomer in the DJ-1 dimer.
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