Members of the NTR/TNFR family mediate apoptosis in many tissues, yet
sequence homology has not been detected in their intracellular domains
except for a 'death domain' in TNFR-I and Fas, Here, a region of the
75 kDa neurotrophin receptor (NTR) has been aligned with this apoptosi
s-inducing motif. Peptides at the carboxyl terminus of each domain pot
entially form amphiphilic helices, one of which (in NTR) resembles mas
toparan, a G-protein activating peptide. Molecular models of three dea
th-region peptides suggest that observed sequence similarities reflect
a common structure, perhaps capable of undergoing an induced coil to
helix transition.