1ibx: Difference between revisions
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'''NMR STRUCTURE OF DFF40 AND DFF45 N-TERMINAL DOMAIN COMPLEX''' | '''NMR STRUCTURE OF DFF40 AND DFF45 N-TERMINAL DOMAIN COMPLEX''' | ||
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[[Category: Wagner, G.]] | [[Category: Wagner, G.]] | ||
[[Category: Zhou, P.]] | [[Category: Zhou, P.]] | ||
[[Category: | [[Category: Cide]] | ||
[[Category: | [[Category: Cide domain complex]] | ||
[[Category: | [[Category: Dff40]] | ||
[[Category: | [[Category: Dff45]] | ||
[[Category: | [[Category: Protein-protein complex]] | ||
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Revision as of 19:49, 2 May 2008
NMR STRUCTURE OF DFF40 AND DFF45 N-TERMINAL DOMAIN COMPLEX
OverviewOverview
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.
About this StructureAbout this Structure
1IBX is a Protein complex structure of sequences from Homo sapiens and Streptococcus sp. and homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45., Zhou P, Lugovskoy AA, McCarty JS, Li P, Wagner G, Proc Natl Acad Sci U S A. 2001 May 22;98(11):6051-5. PMID:11371636 Page seeded by OCA on Fri May 2 19:49:26 2008