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After 1-day transfection, transfected cells were plated onto a 96-well plate treated by cell adherent reagent (Applygen).
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The assays have confirmed that protein- and fat-rich food is the most important stimulus (11, 54). Of the constituents, protein and l -amino acids as well as digested fat cause significant CCK release (54, 55). Carbohydrates only release small amounts of CCK (54), but hydrochloric acid also stimulates release (55). As described earlier (9), “the exomal unit of the CCK gene is seven kilobases interrupted by two introns (23). Whereas the function of the E-box and the GC-rich region is not fully clarified (26, 27), the combined CRE/TRE sequence plays an important role in the regulation of CCK transcription.
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In the CCK2R–Gq complex, Gq undergoes an anticlockwise rotation relative to the receptor compared to Gs (except for EP4R–Gs) (Supplementary Fig. S5a, f). This difference makes the α5 helix of Gq moving closer to the TM2–TM3–TM4 half (Supplementary Fig. S5h, i). It remains mysterious that the CCKRs with highly conserved orthosteric binding pocket display distinct affinity and potency on various endogenous ligands, according to previous homology modeling and mutagenesis studies45.
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Although CCK-8 is located in a similar orthosteric pocket in CCK1R and CCK2R, the binding modes significantly differ (Fig. 2d, e). N982.61 and R197ECL2 form hydrogen bonds with the sulfonic acid group of TYS, vital for CCK-8 binding to CCK1R. The importance of the hydrogen bonds was reflected in our mutagenesis studies, wherein R197ECL2A decreased the potency of CCK-8 by over 100-fold and N982.61A abolished the efficacy (Fig. 2g, h; Supplementary Tables S2, S3). The outward movement of TM6 is a hallmark of receptor activation and the various extent of the TM6 openness relative to other TMs was proposed to be the determinants of G protein subtype specificity47,48. Surprisingly, structural superimposition of the CCK1R–Gs complex onto the well-studied Gs-coupled GPCR β2AR reveals striking differences regarding the position of TM6, and TM7–Helix8 hinge. CCK1R TM6 locates between the positions of β2AR TM6 in the inactive and active states (Fig. 5c).
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