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The concentration increases within 20 min to 3–5 pmol/l during meal stimulation, and then declines gradually only to reach a second peak after 1.5–2 hours. In comparison with most other pancreatic and gastrointestinal hormones (62), the concentrations of CCK in plasma are low. When food-induced CCK in plasma is mimicked by infusion of exogenous CCK, the same degree of gallbladder contraction and release of enzymes as seen during meals occurs (54, 62–64). Therefore, the low circulating concentrations of CCK are sufficient to account for the gallbladder contraction and pancreatic enzyme secretion during meals. The major sites of CCK expression are as mentioned endocrine cells in the gut, the brain, and in peripheral nerves.
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C Superposition of SR activated CCK1R (pink) with active β2AR (dark green) and inactive β2AR (gray). D–g Close-up views of conformational changes in crucial residues involved in CCK1R (pink) and β2AR (dark green) activation. For those who prefer quick and anonymous transactions, Ck444 accepts popular cryptocurrencies like Bitcoin, Ethereum, and Litecoin. Rise to the top of the leaderboard and claim your share of the prize pool with the Ck444 Leaderboard reward.
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The wild-type human CCK1R and CCK2R with C-terminal 15-residue depleted were subcloned into pFastBac vector with an N-terminal FLAG-tag and C-terminal 10× His-tag. A dominant-negative human Gαs (DNGαs) was generated by site-directed mutagenesis as previously described to limit G protein dissociation. Twenty-nine amino acids at the N-terminus of wild-type Gαq were replaced by the corresponding sequence in Gαi1 to facilitate the binding of scFv16. The constructs were cloned into both pcDNA3.1 and pFastBac vectors for functional assays in mammalian cells and protein expression in insect cells, respectively. All modifications of the receptor had no effect on ligand binding and receptor activation.
This smaller opening of the intracellular pocket for G protein is not suitable to engage with the Gs protein due to potential steric hindrance (Supplementary Fig. S5a). The α5 helix of Gαs protein is bulkier than that of other G proteins (Supplementary Fig. S5b) and thus it is believed that the engagement of Gs requires larger outward movement of TM6. Therefore, we hypothesized that the unique conformation of the intracellular half of the active CCK1R would lead to a non-canonical Gs-coupling mode that is elaborated below. This observation also supports the previous hypothesis that the smaller displacement of TM6 in the Gi/o-bound class-A GPCRs might preclude the binding of Gs49.
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