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This relatively small GPCR family is characterized by a long extracellular ligand-binding domain stabilized by three disulfide bridges formed by six highly conserved cysteine residues, seven -helical transmembrane domains, universal for all GPCRs and an intracellular C-terminal domain, responsible mostly for receptor internalization due to the presence of multiple phosphorylation sites [22, 23]

As an important downstream signaling molecule, cAMP is the target of regulation by many receptors after binding their ligands