This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ps4
From Proteopedia
|
crystal structure of DJ-1
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
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 Mon Nov 12 18:46:40 2007
