Identification of a conserved protein motif in a group of growth factor receptors.

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 Lett

journal_title

FEBS letters

authors

Feinstein DL,Larhammar D

doi

10.1016/0014-5793(90)80437-n

subject

Has Abstract

pub_date

1990-10-15 00:00:00

pages

7-11

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(90)80437-N

journal_volume

272

pub_type

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