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1pdw
From Proteopedia
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Crystal structure of human DJ-1, P 1 21 1 space group
Contents |
Overview
We report the crystal structure at 1.8-A resolution of human DJ-1, which, has been linked to early onset Parkinson's disease. The monomer of DJ-1, contains the alpha/beta-fold that is conserved among members of the, DJ-1/ThiJ/PfpI superfamily. However, the structure also contains an extra, helix at the C terminus, which mediates a novel mode of dimerization for, the DJ-1 proteins. A putative active site has been identified near the, dimer interface, and the residues Cys-106, His-126, and Glu-18 may play, important roles in the catalysis by this protein. Studies with the, disease-causing L166P mutant suggest that the mutation has disrupted the, C-terminal region and the dimerization of the protein. The DJ-1 proteins, may function only as dimers. The Lys to Arg mutation at residue 130, the, site of sumoylation of DJ-1, has minimal impact on the structure of the, protein.
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
1PDW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease., Tao X, Tong L, J Biol Chem. 2003 Aug 15;278(33):31372-9. Epub 2003 May 21. PMID:12761214
Page seeded by OCA on Mon Nov 12 18:42:34 2007
Categories: Homo sapiens | Single protein | Tao, X. | Tong, L. | Dj-1
