1IYR

NMR Structure Ensemble Of Dff-C Domain

1IYR の概要

• エントリーDOI: 10.2210/pdb1iyr/pdb
• 関連するPDBエントリー: 1KOY
• 分子名称: DNA FRAGMENTATION FACTOR ALPHA SUBUNIT (1 entity in total)
• 機能のキーワード: dff, apoptosis, riken structural genomics/proteomics initiative, rsgi, structural genomics
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: O00273
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12144.62

構造登録者

Fukushima, K.,Kikuchi, J.,Koshiba, S.,Kigawa, T.,Kuroda, Y.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2002-09-05, 公開日: 2002-09-25, 最終更新日: 2023-12-27)

主引用文献

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

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: 12144788
DOI: 10.1016/S0022-2836(02)00588-0

実験手法

SOLUTION NMR