1IBX

NMR STRUCTURE OF DFF40 AND DFF45 N-TERMINAL DOMAIN COMPLEX

1IBX の概要

• エントリーDOI: 10.2210/pdb1ibx/pdb
• 分子名称: DNA FRAGMENTATION FACTOR 40, CHIMERA OF IGG BINDING PROTEIN G AND DNA FRAGMENTATION FACTOR 45 (2 entities in total)
• 機能のキーワード: dff40, dff45, protein-protein complex, cide, cide domain complex, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25995.31

構造登録者

Zhou, P.,Lugovskoy, A.A.,McCarty, J.S.,Li, P.,Wagner, G. (登録日: 2001-03-29, 公開日: 2001-05-02, 最終更新日: 2024-05-22)

主引用文献

Zhou, P.,Lugovskoy, A.A.,McCarty, J.S.,Li, P.,Wagner, G.
Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45.
Proc.Natl.Acad.Sci.USA, 98:6051-6055, 2001

PubMed Abstract: Apoptotic DNA fragmentation is mediated by a caspase-activated DNA fragmentation factor (DFF)40. Expression and folding of DFF40 require the presence of DFF45, which also acts as a nuclease inhibitor before DFF40 activation by execution caspases. The N-terminal domains (NTDs) of both proteins are homologous, and their interaction plays a key role in the proper functioning of this two-component system. Here we report that the NTD of DFF45 alone is unstructured in solution, and its folding is induced upon binding to DFF40 NTD. Therefore, folding of both proteins regulates the formation of the DFF40/DFF45 complex. The solution structure of the heterodimeric complex between NTDs of DFF40 and DFF45 reported here shows that the mutual chaperoning includes the formation of an extensive network of intermolecular interactions that bury a hydrophobic cluster inside the interface, surrounded by intermolecular salt bridges.

PubMed: 11371636
DOI: 10.1073/pnas.111145098

実験手法

SOLUTION NMR