View source for 1iyr


==NMR Structure Ensemble Of Dff-C Domain==
<StructureSection load='1iyr' size='340' side='right'caption='[[1iyr]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1iyr]] 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=1IYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IYR FirstGlance]. <br>
</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'>[https://proteopedia.org/fgij/fg.htm?mol=1iyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iyr OCA], [https://pdbe.org/1iyr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iyr RCSB], [https://www.ebi.ac.uk/pdbsum/1iyr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iyr ProSAT], [https://www.topsan.org/Proteins/RSGI/1iyr TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DFFA_HUMAN DFFA_HUMAN] Inhibitor of the caspase-activated DNase (DFF40).
<div style="background-color:#fffaf0;">
== 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<ref>PMID:12144788</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1iyr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Fukushima K]]
[[Category: Kigawa T]]
[[Category: Kikuchi J]]
[[Category: Koshiba S]]
[[Category: Kuroda Y]]
[[Category: Yokoyama S]]