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Homodimerization of Human Mu-Opoid Receptor Overexpressed in Sf9 Insect Cells

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In this study, we demonstrate that human mu-opioid receptors do form SDS-resistant homodimers and examine the ability of human mu-opioid receptors to dimerize and the role of agonists in the dimerization. Increasing concentrations and longer exposure of agonists reduce the levels of dimmer with a corresponding increase in the levels of monomer. This effect is achieved with both peptide and alkaloid opioid agonists and it is antagonist reversible. These results suggest that human muopioid receptors are present as receptor oligomers and interconversion between dimeric and monomeric forms may be important for biological activity.

Keywords: alkaloid opioid agonist; homo dimerization; opioid receptor; peptide opioid agonist; receptor oligomer

Document Type: Review Article


Affiliations: Shanghai Institute of Materia Medica, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China

Publication date: April 1, 2002

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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