TY - JOUR
T1 - Molecular basis of agonist binding to the type A cholecystokinin receptor
AU - Miller, Laurence J.
AU - Lybrand, Terry P.
PY - 2002/12/1
Y1 - 2002/12/1
N2 - The receptors for cholecystokinin (CCK) peptides are guanine nucleotide-binding protein-coupled receptors in the rhodopsin/β-adrenergic receptor family. The molecular basis of natural ligand binding to the type A CCK receptor has been studied using ligand structure-activity series, receptor mutagenesis, and photoaffinity labeling studies. These have focused attention on the extracellular loop and tail domains, with the most direct insights coming from intrinsic photoaffinity labeling studies. A model of the binding of CCK to this receptor is consistent with all these studies. This model places the carboxyl terminus of CCK adjacent to the amino-terminal tail outside of transmembrane segment 1, the mid-region of the peptide adjacent to the third extracellular loop outside of transmembrane segment 7, and includes a charge-charge interaction between peptide residue tyrosine-sulfate 27 and the arginine residue in the second extracellular loop of the receptor in position 197.
AB - The receptors for cholecystokinin (CCK) peptides are guanine nucleotide-binding protein-coupled receptors in the rhodopsin/β-adrenergic receptor family. The molecular basis of natural ligand binding to the type A CCK receptor has been studied using ligand structure-activity series, receptor mutagenesis, and photoaffinity labeling studies. These have focused attention on the extracellular loop and tail domains, with the most direct insights coming from intrinsic photoaffinity labeling studies. A model of the binding of CCK to this receptor is consistent with all these studies. This model places the carboxyl terminus of CCK adjacent to the amino-terminal tail outside of transmembrane segment 1, the mid-region of the peptide adjacent to the third extracellular loop outside of transmembrane segment 7, and includes a charge-charge interaction between peptide residue tyrosine-sulfate 27 and the arginine residue in the second extracellular loop of the receptor in position 197.
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U2 - 10.1034/j.1600-0773.2002.910603.x
DO - 10.1034/j.1600-0773.2002.910603.x
M3 - Article
C2 - 12688369
AN - SCOPUS:0036968574
SN - 0901-9928
VL - 91
SP - 282
EP - 285
JO - Pharmacology and Toxicology
JF - Pharmacology and Toxicology
IS - 6
ER -