1koy
From Proteopedia
(New page: 200px<br /> <applet load="1koy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1koy" /> '''NMR structure of DFF-C domain'''<br /> ==O...) |
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| - | [[Image:1koy.gif|left|200px]]<br /> | + | [[Image:1koy.gif|left|200px]]<br /><applet load="1koy" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''NMR structure of DFF-C domain'''<br /> | '''NMR structure of DFF-C domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | DFF45/ICAD has dual functions in the final stage of apoptosis, by acting | + | DFF45/ICAD has dual functions in the final stage of apoptosis, by acting as both a folding chaperone and a DNase inhibitor of DFF40/CAD. Here, we present the solution structure of the C-terminal domain of DFF45, which is essential for its chaperone-like activity. The structure of this domain (DFF-C) consists of four alpha helices, which are folded in a novel helix-packing arrangement. The 3D structure reveals a large cluster of negatively charged residues on the molecular surface of DFF-C. This observation suggests that charge complementation plays an important role in the interaction of DFF-C with the positively charged catalytic domain of DFF40, and thus for the chaperone activity of DFF45. The structure of DFF-C also provides a rationale for the loss of the chaperone activity in DFF35, a short isoform of DFF45. Indeed, in DFF35, the amino acid sequence is truncated in the middle of the second alpha helix constituting the structure of DFF-C, and thus both the hydrophobic core and the cluster of negative charges are disrupted. |
==About this Structure== | ==About this Structure== | ||
| - | 1KOY 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:// | + | 1KOY 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=1KOY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Koshiba, S.]] | [[Category: Koshiba, S.]] | ||
[[Category: Kuroda, Y.]] | [[Category: Kuroda, Y.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
[[Category: apoptosis]] | [[Category: apoptosis]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:30 2008'' |
Revision as of 11:36, 21 February 2008
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NMR structure of DFF-C domain
Overview
DFF45/ICAD has dual functions in the final stage of apoptosis, by acting as both a folding chaperone and a DNase inhibitor of DFF40/CAD. Here, we present the solution structure of the C-terminal domain of DFF45, which is essential for its chaperone-like activity. The structure of this domain (DFF-C) consists of four alpha helices, which are folded in a novel helix-packing arrangement. The 3D structure reveals a large cluster of negatively charged residues on the molecular surface of DFF-C. This observation suggests that charge complementation plays an important role in the interaction of DFF-C with the positively charged catalytic domain of DFF40, and thus for the chaperone activity of DFF45. The structure of DFF-C also provides a rationale for the loss of the chaperone activity in DFF35, a short isoform of DFF45. Indeed, in DFF35, the amino acid sequence is truncated in the middle of the second alpha helix constituting the structure of DFF-C, and thus both the hydrophobic core and the cluster of negative charges are disrupted.
About this Structure
1KOY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the DFF-C domain of DFF45/ICAD. A structural basis for the regulation of apoptotic DNA fragmentation., Fukushima K, Kikuchi J, Koshiba S, Kigawa T, Kuroda Y, Yokoyama S, J Mol Biol. 2002 Aug 9;321(2):317-27. PMID:12144788
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