1pdw: Difference between revisions

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[[Image:1pdw.gif|left|200px]]<br />

[[Image:1pdw.gif|left|200px]]<br /><applet load="1pdw" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1pdw" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1pdw, resolution 2.20Å" />

'''Crystal structure of human DJ-1, P 1 21 1 space group'''<br />

==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.

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==

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==About this Structure==

1PDW 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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1PDW OCA].

1PDW 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=1PDW OCA].

==Reference==

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[[Category: dj-1]]

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@@ Line 1: / Line 1: @@
-[[Image:1pdw.gif|left|200px]]<br />
+[[Image:1pdw.gif|left|200px]]<br /><applet load="1pdw" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1pdw" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1pdw, resolution 2.20&Aring;" />
 '''Crystal structure of human DJ-1, P 1 21 1 space group'''<br />
 ==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.
+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==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-PDW 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PDW OCA].
+PDW 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=1PDW OCA].
 ==Reference==
@@ Line 21: / Line 20: @@
 [[Category: dj-1]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:42:34 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:50 2008''