Abstract
Agonist interaction of all three opioid receptor subtypes μ,δ and can result in the inhibition of adenylate cyclase and/or the regulation of ion channels by activation of one or more pertussis toxin sensitive guanine nucleotide binding proteins (G-proteins) acting as signal transducers (Childers, 1991). Although there has been extensive analysis of opioid receptor function and pharmacology our understanding of the molecular basis of these properties is limited. Recently all subtypes of opioid receptors have been cloned (Evans et al., 1992, Reisine and Bell, 1993 and references therein). Comparison of amino acid sequences of the three cloned opioid receptors reveals high sequence similarity of the intracellular loops suggesting that they might interact with similar G-proteins.
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Georgoussi, Z., Milligan, G., Zioudrou, C. (1995). Identification of stable opioid receptor Go-protein complexes using GTP-binding protein selective antisera. In: Packer, L., Wirtz, K.W.A. (eds) Signalling Mechanisms — from Transcription Factors to Oxidative Stress. NATO ASI Series, vol 92. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-79675-3_9
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DOI: https://doi.org/10.1007/978-3-642-79675-3_9
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