alexa Lipid-mediated dimerization of beta2-adrenergic receptor reveals important clues for cannabinoid receptors.
Pharmaceutical Sciences

Pharmaceutical Sciences

Biochemistry & Pharmacology: Open Access

Author(s): Dainese E, Oddi S, Maccarrone M

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Abstract The high-resolution crystal structure of an engineered human beta2-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 beta2-adrenergic receptor as a template. The structural comparison between the two cannabinoid receptor subtypes and the beta2-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. This article was published in Cell Mol Life Sci and referenced in Biochemistry & Pharmacology: Open Access

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