Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 422, Issue 4, Pages 556-560Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2012.05.023
Keywords
G protein coupled receptors; Mu and delta opioid receptor; Nuclear localization; Protein structure; Heteromer; Interacting amino acids; G protein; Dimers
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Funding
- Canadian Institutes for Health Research
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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. (C) 2012 Elsevier Inc. All rights reserved.
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