Opioid and chemokine receptor heterodimers: arranged marriages or dangerous liaisons?
Heterodimerization of GPCRs (G-protein-coupled receptors) has begun to be appreciated as a rich new vein for drug discovery. The possibility of developing modulators for different GPCRs which work at allosteric sites other than the ligand-binding site is not new, but the notion of using a dimeric receptor partner as the target for this intervention has not yet percolated into the broader industrial community. In the present article, I discuss this notion in the context of the heterodimeric delta-opioid receptor-CXCR2 chemokine receptor dimer identified by Parenty et al., in this issue of the Biochemical Journal.
Hébert
Terence E
TE
Department of Pharmacology and Therapeutics, Faculty of Medicine, 13th floor, Room 1303, McIntyre Medical Sciences Building, 3655 Promenade Sir William Osler, Montreal, QC, Canada, H3G 1Y6. terence.hebert@mcgill.ca
D019281:Dimerization; D006801:Humans; D020836:Protein Structure, Quaternary; D023063:Receptors, Interleukin-8B / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017465:Receptors, Opioid, delta / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D023063:Receptors, Interleukin-8B; D017465:Receptors, Opioid, delta; D011993:Recombinant Fusion Proteins