The catecholamine binding site of the β-adrenergic receptor is formed by juxtaposed membrane-spanning domains

S. K F Wong, Clive A. Slaughter, A. E. Ruoho, E. M. Ross

Research output: Contribution to journalArticle

85 Scopus citations

Abstract

The catecholamine binding domain of the turkey erythrocyte β-adrenergic receptor was mapped by determining the sites of covalent labeling of the purified receptor by two β-adrenergic photoaffinity reagents, [125I]iodocyanopindolol-diazirine (ICYP-da) and [125I]iodoazidobenzylpindolol (IABP). Both labels were incorporated at two separate sites. By sequencing a labeled peptide, one site of labeling was found to lie at Trp330 in the extracellular half of the seventh membrane span. This position is homologous to the retinal attachment site in rhodopsin. The second labeled site was isolated on an 8000-Da peptide and immunoprecipitated using sequence-directed antibodies. This site lies in membrane spans 3-5. Labeling of the two sites was equal using ICYP-da and 3-10-fold greater in the span 7 site using IABP. These data indicate that the catecholamine binding site is formed from the juxtaposition of span 7 and spans 3-5 in a tertiary structure probably similar to that of rhodopsin.

Original languageEnglish (US)
Pages (from-to)7925-7928
Number of pages4
JournalJournal of Biological Chemistry
Volume263
Issue number17
Publication statusPublished - Jan 1 1988
Externally publishedYes

    Fingerprint

ASJC Scopus subject areas

  • Biochemistry

Cite this