The avian β-adrenergic receptor: primary structure and membrane topology

Yarden, Y. ; Rodriguez, H. ; Wong, S. K. ; Brandt, D. R. ; May, D. C. ; Burnier, J. ; Harkins, R. N. ; Chen, E. Y. ; Ramachandran, J. ; Ullrich, A. ; Ross, E. M. (1986) The avian β-adrenergic receptor: primary structure and membrane topology PNAS, 83 (18). pp. 6795-6799. ISSN 0027-8424

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Partial amino acid sequence information allowed the isolation of cDNA clones encoding the turkey erythrocyte β-adrenergic receptor. Antisera raised against synthetic peptides encoded by the cDNA crossreacted with the purified receptor and appropriate tryptic fragments, confirming the identity of the cDNA. The receptor is composed of 483 amino acids and has a molecular mass of 54 kDa. Its sequence suggests that it is arranged predominantly in seven membrane-spanning sequences and a long cytoplasmic carboxyl-terminal domain. The extracellular amino-terminal domain contains a consensus sequence for N-glycosylation. The β-adrenergic receptor displays overall structural similarity and weak sequence homology with rhodopsin. Because both proteins act by regulating GTP-binding proteins, a compact structure based on seven membrane-spanning regions may be a general model for receptors that act on G proteins.

Item Type:Article
Source:Copyright of this article belongs to National Academy of Sciences.
ID Code:40725
Deposited On:25 May 2011 05:26
Last Modified:17 May 2016 22:42

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