Abstract
Like several other members of the G-protein coupled receptor (GPCR) family, opioid receptors interact among themselves at the plasma membrane to form dimers/oligomers. Despite recent compelling evidence for the involvement of transmembrane (TM) regions at the dimerization/oligomerization interface of GPCRs, the specific residues in contact are unknown for most receptors, including the opioid receptor subtypes. Based on prior inferences from correlated mutation analysis, we performed experimental testing of the interfaces of delta- (DOR) and mu- (MOR) opioid receptor oligomers by carrying out cross-linking studies on a series of substituted cysteines in TM1, 4 and 5.
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