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Role of the extracellular domains of the cholecystokinin receptor in agonist binding.
TLDR
The data suggest that CCK-8 interacts at multiple contact points in the extracellular domains of CCK receptors and that the CCKAR and CCKBR have distinct binding sites despite their shared high affinity for CCk-8.
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Identification of Two Amino Acids of the Human Cholecystokinin-A Receptor That Interact with the N-terminal Moiety of Cholecystokinin*
TLDR
The modeling of the CCK-A receptor and the docking of the peptide agonists indicated that their N terminus was connected to the receptor through a strong bond network involving Trp-39 and Gln-40 thus confirming experimental data, an important step toward the complete delineation of the agonist binding site.
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Rhodopsin crystal: new template yielding realistic models of G-protein-coupled receptors?
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Probing a model of a GPCR/ligand complex in an explicit membrane environment: the human cholecystokinin-1 receptor.
TLDR
It is proposed that this detailed consistency-checking procedure be used as a routine refinement step of in vacuo GPCR models, before further investigation and application to structure-based drug design.
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Insights into the binding and activation sites of the receptors for cholecystokinin and gastrin
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Evidence for a functional role of the cholecystokinin-B/gastrin receptor in the human fetal and adult pancreas.
TLDR
Data presented are consistent with the view that the CCK-B/G receptor is involved in glucose homeostasis in adult humans and mediates the autocrine effects of G on islet differentiation and growth in the fetal pancreas.
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Arginine 336 and Asparagine 333 of the Human Cholecystokinin-A Receptor Binding Site Interact with the Penultimate Aspartic Acid and the C-terminal Amide of Cholecystokinin*
TLDR
The identified interactions are crucial for stabilizing the high affinity phospholipase C-coupled state of the CCK-AR·CCK complex, and Arg-336 and Asn-333 are directly involved in interactions with nonpeptide antagonists SR-27,897 and L-364,718.
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Met-195 of the Cholecystokinin-A Receptor Interacts with the Sulfated Tyrosine of Cholecystokinin and Is Crucial for Receptor Transition to High Affinity State*
TLDR
Using three-dimensional modeling, methionine 195 of the CCK-A receptor is identified as a putative amino acid in interaction with the aromatic ring of the sulfated tyrosine of CCK to correctly position the sulfation group ofCCK in the binding site of the receptor.
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Arginine 197 of the cholecystokinin‐A receptor binding site interacts with the sulfate of the peptide agonist cholecystokinin
TLDR
Data support an interaction between Arg 197 of the CCK‐AR binding site and the sulfate of CCK, suggesting that Arg 197‐sulfate interaction regulates conformational changes of the CCP‐AR that are required for its physiological activation.
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The Biologically Crucial C Terminus of Cholecystokinin and the Non-peptide Agonist SR-146,131 Share a Common Binding Site in the Human CCK1 Receptor
TLDR
Mapping of the CCK1R binding site by identifying residues that interact with the methionine and phenylalanine residues of the C-terminal moiety of CCK because these are crucial for its binding and biological activity and to determine whether CCK and the selective non-peptide agonist, SR-146,131, share a common binding site.
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