Lipid-mediated dimerization of β2-adrenergic receptor reveals important clues for cannabinoid receptors

E. Dainese, S. Oddi, M. Maccarrone

Research output: Contribution to journalArticlepeer-review


The high-resolution crystal structure of an engineered human β2-adrenergic receptor has recently been resolved, suggesting a molecular mechanism by which cholesterol may mediate receptor dimerization. Here, we present a critical examination of new structural and functional insights derived from unprecedented preliminary homology modeling of cannabinoid receptors, obtained using the crystal structure of β2- adrenergic receptor as a template. The structural comparison between the two cannabinoid receptor subtypes and the β2-adrenergic receptor may be of particular interest, by providing important clues for the elucidation of the structural determinants involved in cholesterol binding. In addition, the implications of G protein coupled receptor dimerization, as well as the role of cholesterol in this process, are briefly discussed.

Original languageEnglish
Pages (from-to)2277-2279
Number of pages3
JournalCellular and Molecular Life Sciences
Issue number15
Publication statusPublished - Aug 2008


  • β-adrenergic receptor
  • Cannabinoid receptors
  • Cholesterol
  • Lipid binding domain
  • Receptor dimerization

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Cell Biology


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