Journal article icon

Journal article

The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations.

Abstract:

The death-inducing signaling complex (DISC) formed by the death receptor Fas, the adaptor protein FADD and caspase-8 mediates the extrinsic apoptotic program. Mutations in Fas that disrupt the DISC cause autoimmune lymphoproliferative syndrome (ALPS). Here we show that the Fas-FADD death domain (DD) complex forms an asymmetric oligomeric structure composed of 5-7 Fas DD and 5 FADD DD, whose interfaces harbor ALPS-associated mutations. Structure-based mutations disrupt the Fas-FADD interaction...

Expand abstract
Publication status:
Published

Actions


Access Document


Publisher copy:
10.1038/nsmb.1920

Authors


Expand authors...
Journal:
Nature structural and molecular biology
Volume:
17
Issue:
11
Pages:
1324-1329
Publication date:
2010-11-05
DOI:
EISSN:
1545-9985
ISSN:
1545-9993
URN:
uuid:dd1f102c-98fd-4985-be48-8f47b151fca4
Source identifiers:
97315
Local pid:
pubs:97315

Terms of use


Metrics


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