Article
Solution NMR investigation of the CD95/FADD homotypic death domain complex suggests lack of engagement of the CD95 C terminus.
Structure (London, England : 1993) - 13 Oct 2010
Esposito Diego, Sankar Andrew, Morgner Nina, Robinson Carol V, Rittinger Katrin, Driscoll Paul C
Abstract excerpt
We have addressed complex formation between the death domain (DD) of the death receptor CD95 (Fas/APO-1) with the DD of immediate adaptor protein FADD using nuclear magnetic resonance (NMR) spectroscopy, mass spectrometry, and size-exclusion chromatography with in-line light scattering. We find complexation to be independent of the C-terminal 12 residues of CD95 and insensitive to mutation of residues that engage...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.