Design: An assay based on single-polypeptide-chain heterodimeric A2AR/D2R and non-oligomerized fusions for in vivo analysis of their allosteric receptor-receptor interactions

BioRxiv : the Preprint Server for Biology
Toshio KamiyaHiroyasu Nakata


Background: The adenosine A2A receptor (A2AR) heteromerizes with the dopamine D2 receptor (D2R). In order to explore their functional interaction, we engineered previously stable single-polypeptide-chain (sc) A2AR/D2LR: whether the molecular entity of the striatal A2AR/D2R antagonism, i.e., scA2AR/D2Rs are just A2AR/D2R with the antagonism, remains unresolved. New Method: To further clarify the heteromerization through the scA2AR/D2LR, we here designed supramolecularly ˋexclusiveˊ monomers and dimers, using the Cϵ2 domain of IgE-Fc or apoproteins of the bacterial light-harvesting antenna complex. Results: A concept of the recptor protein assembly regulation, i.e., the selective monomer/non-obligate dimer formation was obtained. Although none of these new fusions were constructed or tested, we could aim at obtaining heterodimer-specific agents, using the scA2AR/D2R. Whether the resulting designs were explained feasibly and rationally was addressed. The structure and function of the non-obligate dimer were here discussed through scA2AR/D2R, focusing on the procedure of the membrane protein design and methods for transient protein-protein interactions. Summary and Outlook: Given that upon being expressed and allosteric regulation ...Continue Reading

Related Concepts

Allosteric Regulation
Corpus Striatum Structure
Membrane Proteins
Physiological Aspects
Dopamine D2 Receptor
Adenosine A2A Receptor

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