1IBX

NMR STRUCTURE OF DFF40 AND DFF45 N-TERMINAL DOMAIN COMPLEX

Summary for 1IBX

• Entry DOI: 10.2210/pdb1ibx/pdb
• Descriptor: DNA FRAGMENTATION FACTOR 40, CHIMERA OF IGG BINDING PROTEIN G AND DNA FRAGMENTATION FACTOR 45 (2 entities in total)
• Functional Keywords: dff40, dff45, protein-protein complex, cide, cide domain complex, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 25995.31

Authors

Zhou, P.,Lugovskoy, A.A.,McCarty, J.S.,Li, P.,Wagner, G. (deposition date: 2001-03-29, release date: 2001-05-02, Last modification date: 2024-05-22)

Primary citation

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

Experimental method

SOLUTION NMR