Abstract:
:Fas and its ligand (FasL) are members of the tumor necrosis factor receptor (TNFR) and tumor necrosis factor (TNF) superfamilies, respectively. Fas-FasL interactions trigger controlled cell death (apoptosis) in the immune system and thus play a key role in the regulation of immune responses. Structural details of the Fas-Fas ligand interaction are currently unknown. Previously, six Fas residues were identified by mutagenesis as important for ligand binding. We have now extended our mutagenesis analysis and identified additional residues which contribute to the Fas-FasL interaction. Candidate and control residues were selected based on a molecular model of the Fas extracellular region. Although residues in all three extracellular domains were identified to contribute to binding, the Fas-FasL interaction is centered on the second TNFR-like domain. Important residues were compared to critical positions in TNFR and CD40, another member of the TNFR family.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Starling GC,Kiener PA,Aruffo A,Bajorath Jdoi
10.1021/bi972959dsubject
Has Abstractpub_date
1998-03-17 00:00:00pages
3723-6issue
11eissn
0006-2960issn
1520-4995pii
bi972959djournal_volume
37pub_type
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