Journal article icon

Journal article

Solution NMR investigation of the CD95/FADD homotypic death domain complex suggests lack of engagement of the CD95 C terminus.

Abstract:

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 in the high-order clustering of CD95-DD molecules in a recently reported crystal...

Expand abstract
Publication status:
Published

Actions


Access Document


Publisher copy:
10.1016/j.str.2010.08.006

Authors


Expand authors...
Journal:
Structure (London, England : 1993)
Volume:
18
Issue:
10
Pages:
1378-1390
Publication date:
2010-10-01
DOI:
EISSN:
1878-4186
ISSN:
0969-2126
Source identifiers:
93316

Terms of use


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP