Disruption of the mu-delta opioid receptor heteromer.

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

Disruption of the mu-delta opioid receptor heteromer.

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

Permalink

Publication Type:: Journal Article
Citation:: Biochemical and biophysical research communications, 2012, 422 (4), pp. 556 - 560
Issue Date:: 2012-06

Closed Access

	Filename	Description	Size
	1-s2.0-S0006291X1200887X-main.pdf	Published Version	718.34 kB	Adobe PDF	View/Open

Copyright Clearance Process

Recently Added
In Progress
Closed Access

This item is closed access and not available.

Full metadata record

Field	Value	Language
dc.contributor.author	O'Dowd, BF	en_US
dc.contributor.author	Ji, X	en_US
dc.contributor.author	O'Dowd, PB	en_US
dc.contributor.author	Nguyen, T	en_US
dc.contributor.author	George, SR	en_US
dc.date.available	2012-05-04	en_US
dc.date.issued	2012-06	en_US
dc.identifier.citation	Biochemical and biophysical research communications, 2012, 422 (4), pp. 556 - 560	en_US
dc.identifier.issn	0006-291X	en_US
dc.identifier.uri	http://hdl.handle.net/10453/113795
dc.description.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.	en_US
dc.format	Print-Electronic	en_US
dc.language	eng	en_US
dc.relation.ispartof	Biochemical and biophysical research communications	en_US
dc.relation.isbasedon	10.1016/j.bbrc.2012.05.023	en_US
dc.subject.classification	Biochemistry & Molecular Biology	en_US
dc.subject.mesh	Cell Line	en_US
dc.subject.mesh	Cell Nucleus	en_US
dc.subject.mesh	Cytoplasm	en_US
dc.subject.mesh	Animals	en_US
dc.subject.mesh	Humans	en_US
dc.subject.mesh	Rats	en_US
dc.subject.mesh	Receptors, Opioid, delta	en_US
dc.subject.mesh	Receptors, Opioid, mu	en_US
dc.subject.mesh	Sequence Analysis, Protein	en_US
dc.subject.mesh	Amino Acid Sequence	en_US
dc.subject.mesh	Protein Transport	en_US
dc.subject.mesh	Molecular Sequence Data	en_US
dc.subject.mesh	Protein Multimerization	en_US
dc.title	Disruption of the mu-delta opioid receptor heteromer.	en_US
dc.type	Journal Article
utslib.citation.volume	4	en_US
utslib.citation.volume	422	en_US
utslib.for	0304 Medicinal And Biomolecular Chemistry	en_US
utslib.for	0601 Biochemistry And Cell Biology	en_US
utslib.for	1101 Medical Biochemistry And Metabolomics	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Engineering and Information Technology
pubs.organisational-group	/University of Technology Sydney/Faculty of Engineering and Information Technology/School of Biomedical Engineering
pubs.organisational-group	/University of Technology Sydney/Strength - CHT - Health Technologies
utslib.copyright.status	closed_access
pubs.declined	2017-07-29T10:22:50.824+1000
pubs.issue	4	en_US
pubs.publication-status	Published	en_US
pubs.volume	422	en_US

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.

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/113795