1pdv
From Proteopedia
(New page: 200px<br /> <applet load="1pdv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pdv, resolution 1.80Å" /> '''Crystal structure o...) |
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| - | [[Image:1pdv.gif|left|200px]]<br /> | + | [[Image:1pdv.gif|left|200px]]<br /><applet load="1pdv" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1pdv, resolution 1.80Å" /> | caption="1pdv, resolution 1.80Å" /> | ||
'''Crystal structure of human DJ-1, P 31 2 1 space group'''<br /> | '''Crystal structure of human DJ-1, P 31 2 1 space group'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We report the crystal structure at 1.8-A resolution of human DJ-1, which | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PDV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1PDV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PDV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: dj-1]] | [[Category: dj-1]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:46 2008'' |
Revision as of 12:27, 21 February 2008
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Crystal structure of human DJ-1, P 31 2 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
1PDV 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 Thu Feb 21 14:27:46 2008
Categories: Homo sapiens | Single protein | Tao, X. | Tong, L. | Dj-1
