Disruption of the mu-delta opioid receptor heteromer

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• 作者：Brian F. O&rsquo ; Dowd^a ; ^b ; ^{brian.odowd@utoronto.ca} ; Xiaodong Ji^b ; Paul B. O&rsquo ; Dowd^b ; Tuan Nguyen^a ; ^b ; Susan R. George^a ; ^b ; ^c
• 关键词：G protein coupled receptors ; Mu and delta opioid receptor ; Nuclear localization ; Protein structure ; Heteromer ; Interacting amino acids ; G protein ; Dimers
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2012
• 出版时间：15 June, 2012
• 年：2012
• 卷：422
• 期：4
• 页码：556-560
• 全文大小：718 K

文摘

The crystal structure of the mu and kappa opioid receptors has revealed dimeric structural arrangements. Mu-delta receptors heteromers also exist and we have identified discrete cytoplasmic regions in each receptor required for oligomer formation. In the carboxyl tail of the delta receptor we identified three glycine residues (-GGG), substitution of any of these residues prevented heteromer formation. In intracellular loop 3 of both mu and delta receptors we identified three residues (-SVR), substitution of any of these residues prevented heteromer formation.