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 cck444 ligands, according to previous homology modeling and mutagenesis studies45.
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For the SR146131–CCK1R–Gs–Nb35 complex, auto-picking-yielded 5,213,984 particle projections were subjected to 3D classification to discard particles in poorly defined classes, producing 898,915 particle projections. The re-picked particles were extracted and subjected to two rounds of 3D classification with four classes; the best-resolved class was selected each time. The resulting set of 606,684 particles was subjected to CTF refinement, Bayesian polishing and 3D auto refinement using the pixel size of 1.014 Å. The final map has an indicated global resolution of 3.0 Å at an FSC of 0.143. For the CCK-8–CCK1R–Gs–Nb35 complex, auto-picking-yielded 5,768,688 particle projections were subjected to 3D classification to discard particles in poorly defined classes, producing 1,608,563 particle projections.
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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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The long history has made the CCK literature comprehensive and at some points also confusing because impure CCK preparations with little attention paid to species differences and to physiological levels were used initially. In addition, most assays for measurement of CCK in plasma and elsewhere lacked specificity and sensitivity (10–12). The cellular effects of CCK peptides are mediated via two receptors (66, 67). CCK1 receptors have been found also in the anterior pituitary, the myenteric plexus, and areas of the midbrain (69, 70). The CCK1 receptor binds with high affinity CCK peptides that are amidated and sulfated, whereas the affinity for non-sulfated CCK peptides and gastrins is negligible. In the basal state, the concentration of CCK in plasma is around 1 pmol/l, but often less.
According to the two CCK-8-bound structures, the interfaces between CCK-8 and CCKRs and the overall shape of the orthostatic pockets are conserved, consistent with previous prediction45. However, the sub-pocket for the TYS of CCK-8 is more positively charged in CCK1R attributed to N982.61, and R197ECL2 contributes to a beneficial charge–charge interaction with TYS of CCK-8 (Fig. 3a). Site-directed mutations R197ECL2M/A or N982.61A in CCK1R almost abolished CCK-8-triggered activation, implying the critical role of ECL2 in sulfated endogenous ligand recognition (Fig. 3b). The substitution of Q204ECL2A, the closest polar residue in CCK2R compared to CCK-8, does not affect CCK-8-induced Gq signaling of CCK2R measured by NanoBiT assay (Fig. 3d).
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