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| | ==NMR structure of DFF-C domain== | | ==NMR structure of DFF-C domain== |
| - | <StructureSection load='1koy' size='340' side='right'caption='[[1koy]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='1koy' size='340' side='right'caption='[[1koy]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1koy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KOY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1koy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KOY FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iyr|1iyr]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1koy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1koy OCA], [http://pdbe.org/1koy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1koy RCSB], [http://www.ebi.ac.uk/pdbsum/1koy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1koy ProSAT], [http://www.topsan.org/Proteins/RSGI/1koy TOPSAN]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1koy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1koy OCA], [https://pdbe.org/1koy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1koy RCSB], [https://www.ebi.ac.uk/pdbsum/1koy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1koy ProSAT], [https://www.topsan.org/Proteins/RSGI/1koy TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DFFA_HUMAN DFFA_HUMAN]] Inhibitor of the caspase-activated DNase (DFF40). | + | [https://www.uniprot.org/uniprot/DFFA_HUMAN DFFA_HUMAN] Inhibitor of the caspase-activated DNase (DFF40). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fukushima, K]] | + | [[Category: Fukushima K]] |
| - | [[Category: Kigawa, T]] | + | [[Category: Kigawa T]] |
| - | [[Category: Kikuchi, J]] | + | [[Category: Kikuchi J]] |
| - | [[Category: Koshiba, S]] | + | [[Category: Koshiba S]] |
| - | [[Category: Kuroda, Y]] | + | [[Category: Kuroda Y]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Yokoyama S]] |
| - | [[Category: Yokoyama, S]] | + | |
| - | [[Category: Apoptosis]]
| + | |
| - | [[Category: Dff]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| Structural highlights
Function
DFFA_HUMAN Inhibitor of the caspase-activated DNase (DFF40).
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fukushima K, Kikuchi J, Koshiba S, Kigawa T, Kuroda Y, Yokoyama S. Solution structure of the DFF-C domain of DFF45/ICAD. A structural basis for the regulation of apoptotic DNA fragmentation. J Mol Biol. 2002 Aug 9;321(2):317-27. PMID:12144788
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