Identification of a conserved protein motif in a group of growth factor receptors.
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 alpha-helices, as is the amino-terminal region of the third intracytoplasmic loop (i3) of the beta 2-adrenergic receptor (beta 2AR). As both mastoparan and the beta 2AR 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.
Feinstein
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Institut de Physiologie, Faculté de Médicine, Université de Lausanne, Switzerland.
Larhammar
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D000595:Amino Acid Sequence; D019204:GTP-Binding Proteins / Q000378:metabolism; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D010455:Peptides; D011487:Protein Conformation; D011943:Receptors, Adrenergic, beta / Q000737:chemistry / Q000378:metabolism; D011986:Receptors, Somatotropin / Q000737:chemistry*; D012689:Sequence Homology, Nucleic Acid; D014862:Wasp Venoms / Q000737:chemistry
D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; D011943:Receptors, Adrenergic, beta; D011986:Receptors, Somatotropin; D014862:Wasp Venoms; C037500:mastoparan; D019204:GTP-Binding Proteins