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1pe0
From Proteopedia
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[[Image:1pe0.gif|left|200px]] | [[Image:1pe0.gif|left|200px]] | ||
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'''Crystal structure of the K130R mutant of human DJ-1''' | '''Crystal structure of the K130R mutant of human DJ-1''' | ||
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[[Category: Tao, X.]] | [[Category: Tao, X.]] | ||
[[Category: Tong, L.]] | [[Category: Tong, L.]] | ||
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Revision as of 01:58, 3 May 2008
Crystal structure of the K130R mutant of human DJ-1
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.
About this Structure
1PE0 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 Sat May 3 04:58:49 2008
Categories: Homo sapiens | Single protein | Tao, X. | Tong, L. | Dj-1
