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Identification of a conserved protein motif in a group of growth factor receptors
Author(s) -
Feinstein Douglas L.,
Larhammar Dan
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80437-n
Subject(s) - mastoparan , receptor , structural motif , cytoplasm , signal transduction , biology , sequence motif , g protein , peptide sequence , biochemistry , microbiology and biotechnology , chemistry , gene
Residues 370–383 (helix C) of the human nerve growth factor receptor (NGF‐R) are highly similar to the sequence of the 14 residue wasp toxin, mastoparan. Both regions are predicted to form amphiphilic α‐helices, as is the amino‐terminal region of the third intracytoplasmic loop (i3) of the β 2 ‐adrenergic receptor (β 2 AR). As both mastoparan and the β 2 AR i3 interact with G‐proteins, it is suggested that helix C of the NGF‐R may facilitate interactions with a cytoplasmic protein. A similar structural motif was identified in the cytoplasmic domains of a number of other growth factor receptors, suggesting an important role for this motif in signal transduction mechanisms.