1IYR
NMR Structure Ensemble Of Dff-C Domain
Summary for 1IYR
| Entry DOI | 10.2210/pdb1iyr/pdb |
| Related | 1KOY |
| Descriptor | DNA FRAGMENTATION FACTOR ALPHA SUBUNIT (1 entity in total) |
| Functional Keywords | dff, apoptosis, riken structural genomics/proteomics initiative, rsgi, structural genomics |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: O00273 |
| Total number of polymer chains | 1 |
| Total formula weight | 12144.62 |
| Authors | Fukushima, K.,Kikuchi, J.,Koshiba, S.,Kigawa, T.,Kuroda, Y.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2002-09-05, release date: 2002-09-25, Last modification date: 2023-12-27) |
| Primary citation | 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., 321:317-327, 2002 Cited by PubMed Abstract: 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. PubMed: 12144788DOI: 10.1016/S0022-2836(02)00588-0 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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