Putative cytoplasmic amphiphilic domains in the nerve growth factor/tumour necrosis factor receptor superfamily.
Potential alpha-helical regions in cytoplasmic domains of the NGF/TNF receptor superfamily were searched to identify amphiphilic sequences favouring association with membrane surfaces, analogous to the predicted secondary structure of mastoparan (MP). Similar to MP, NGFR (rat, chick, human), human TNFR-1, and human 4-1BB have domains with putative surface membrane associating sequences. The circular dichroism spectra of mastoparan and a peptide homologous to the putative amphiphilic domain of NGFR were identical in an aqueous milieu, and both adopted an alpha-helical conformation in trifluoroethanol.
Myers
S M
SM
Department of Medicine, Queen's University, Kingston, Ont., Canada.
Ross
G M
GM
Dostaler
S M
SM
Anderson
M N
MN
Weaver
D F
DF
Riopelle
R J
RJ
D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000737:chemistry; D002942:Circular Dichroism; D003593:Cytoplasm / Q000737:chemistry*; D036341:Intercellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017475:Receptors, Nerve Growth Factor / Q000737:chemistry*; D018124:Receptors, Tumor Necrosis Factor / Q000737:chemistry*; D014862:Wasp Venoms / Q000737:chemistry
D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; D017475:Receptors, Nerve Growth Factor; D018124:Receptors, Tumor Necrosis Factor; D014862:Wasp Venoms; C037500:mastoparan