title: Disruption of the mu-delta opioid receptor heteromer.
abstract: 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.
authors.affiliation: Centre for Addiction and Mental Health, University of Toronto, Toronto, Ontario, Canada M5S 1A8. brian.odowd@utoronto.ca
authors.forename: Brian F
authors.initials: BF
authors.lastname: O'Dowd
authors.forename: Xiaodong
authors.initials: X
authors.lastname: Ji
authors.forename: Paul B
authors.initials: PB
authors.lastname: O'Dowd
authors.forename: Tuan
authors.initials: T
authors.lastname: Nguyen
authors.forename: Susan R
authors.initials: SR
authors.lastname: George
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D002467:Cell Nucleus / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D055503:Protein Multimerization; D021381:Protein Transport; D051381:Rats; D017465:Receptors, Opioid, delta / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017450:Receptors, Opioid, mu / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D020539:Sequence Analysis, Protein
chemical_list: D017465:Receptors, Opioid, delta; D017450:Receptors, Opioid, mu