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

Abstract

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
Apoproteins
Corpus Striatum Structure
Dopamine
Flucytosine
Membrane Proteins
Physiological Aspects
Dopamine D2 Receptor
Adenosine A2A Receptor
Dimer

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