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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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

O'Dowd BF,Ji X,O'Dowd PB,Nguyen T,George SR

doi

10.1016/j.bbrc.2012.05.023

subject

Has Abstract

pub_date

2012-06-15 00:00:00

pages

556-60

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(12)00887-X

journal_volume

422

pub_type

杂志文章

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