1koy
From Proteopedia
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| - | [[Image:1koy.gif|left|200px]] | + | [[Image:1koy.gif|left|200px]] |
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| - | '''NMR structure of DFF-C domain''' | + | {{Structure |
| + | |PDB= 1koy |SIZE=350|CAPTION= <scene name='initialview01'>1koy</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NMR structure of DFF-C domain''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1KOY is a [ | + | 1KOY is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12144788 12144788] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:20:14 2008'' |
Revision as of 10:20, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
Page seeded by OCA on Thu Mar 20 12:20:14 2008
