Guanine nucleotide-mediated inhibition of opioid agonist binding: Modulatory effects of ions and of receptor occupancy
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Purification and functional reconstitution of monomeric μ-opioid receptors. Allosteric modulation of agonists binding by G<inf>i2</inf>
2009, Journal of Biological ChemistryCitation Excerpt :The potency and efficacy of DAMGO at insect cell expressed YMOR is well in line with its observed pharmacological characteristics in mammalian cell expression systems (23–25). Allosteric regulation of agonist binding to opioid receptors by G proteins has been well established in plasma membrane preparations of brain homogenates and overexpression systems (26–30) and was also observed for YMOR expressed in insect cells. In the absence of Gi2, DAMGO competed [3H]DPN (0.5 nm) binding in a concentration-dependent manner with a Ki of ∼580 nm (Fig. 1D).
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Present address: Department of Biopharmacy, Institute of Pharmacy, ETHZ, Clausiusstrasse 25, CH-8092 Zürich, Switzerland.
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