Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Feinstein DL,Larhammar Ddoi
10.1016/0014-5793(90)80437-nsubject
Has Abstractpub_date
1990-10-15 00:00:00pages
7-11issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(90)80437-Njournal_volume
272pub_type
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