1q2u
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(New page: 200px<br /> <applet load="1q2u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q2u, resolution 1.6Å" /> '''Crystal structure of...)
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Revision as of 16:43, 12 November 2007
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Crystal structure of DJ-1/RS and implication on familial Parkinson's disease
Contents |
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.
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
1Q2U 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
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