Abstract

The functional importance of G protein-coupled receptor (GPCR) oligomerization remains controversial. Although obligate dimers of class C GPCRs are well accepted, the generalizability of this phenomenon is still strongly debated with respect to other classes of GPCRs. In this review, we focus on understanding the organization and dynamics between receptor equivalents and their signaling partners in oligomeric receptor complexes, with a view toward integrating disparate viewpoints into a unified understanding. We discuss the nature of functional oligomeric entities, and how asymmetries in receptor structure and function created by oligomers might have implications for receptor function as allosteric machines and for future drug discovery.

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