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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Revision as of 15:46, 12 November 2007
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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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