1ps4
From Proteopedia
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'''crystal structure of DJ-1''' | '''crystal structure of DJ-1''' | ||
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[[Category: Sun, Y.]] | [[Category: Sun, Y.]] | ||
[[Category: Wang, H.]] | [[Category: Wang, H.]] | ||
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| - | [[Category: | + | [[Category: Parkinson's disease]] |
| - | [[Category: | + | [[Category: Regulatory protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:25:30 2008'' | |
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Revision as of 02:25, 3 May 2008
crystal structure of DJ-1
Overview
DJ-1 is a protein involved in multiple physiological processes, including cancer, Parkinson's disease, and male fertility. It is unknown how DJ-1 functions in the apparently different systems. The crystal structure of DJ-1 at 1.6 A resolution shows that DJ-1 is a helix-strand-helix sandwich and forms a dimer. The DJ-1 structure is similar to the members of the intracellular protease PfpI family. However, the catalytic triad of Cys-His-Glu is not strictly conserved in DJ-1, implying that DJ-1 has a different catalytic mechanism if it acts as a protease or DJ-1 serves as a regulatory protein in the physiological processes. The structure shows that Leu166 positions in the middle of a helix and thus predicts that the L166P mutation will bend the helix and impact the dimerization of DJ-1. As a result, the conformational changes may diminish the DJ-1 binding with its partner, leading to the familial Parkinson's disease caused by the single L166P mutation.
About this Structure
1PS4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of DJ-1/RS and implication on familial Parkinson's disease., Huai Q, Sun Y, Wang H, Chin LS, Li L, Robinson H, Ke H, FEBS Lett. 2003 Aug 14;549(1-3):171-5. PMID:12914946 Page seeded by OCA on Sat May 3 05:25:30 2008
