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1koy

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(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 />
 
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<applet load="1koy" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1koy" />
 
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'''NMR structure of DFF-C domain'''<br />
 
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==Overview==
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==NMR structure of DFF-C domain==
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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.
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<StructureSection load='1koy' size='340' side='right'caption='[[1koy]]' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DFFA_HUMAN DFFA_HUMAN] Inhibitor of the caspase-activated DNase (DFF40).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:12144788</ref>
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KOY OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12144788 12144788]
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</div>
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<div class="pdbe-citations 1koy" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Fukushima, K.]]
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[[Category: Fukushima K]]
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[[Category: Kigawa, T.]]
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[[Category: Kigawa T]]
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[[Category: Kikuchi, J.]]
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[[Category: Kikuchi J]]
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[[Category: Koshiba, S.]]
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[[Category: Koshiba S]]
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[[Category: Kuroda, Y.]]
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[[Category: Kuroda Y]]
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[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
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[[Category: Yokoyama S]]
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[[Category: Yokoyama, S.]]
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[[Category: apoptosis]]
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[[Category: dff]]
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[[Category: riken structural genomics/proteomics initiative]]
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[[Category: rsgi]]
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[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:53:10 2007''
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Current revision

NMR structure of DFF-C domain

PDB ID 1koy

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