Molecular basis of agonist binding to the type A cholecystokinin receptor.
Molecular basis of agonist binding to the type A cholecystokinin receptor.
复制标题
激动剂与 A 型胆囊收缩素受体结合的分子基础。
DOI：
10.1034/j.1600-0773.2002.910603.x
复制
发表时间：
2002
期刊：
影响因子：
--
通讯作者：
Lybrand,TerryP
中科院分区：
文献类型：
--
作者：
Miller,LaurenceJ;Lybrand,TerryP
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.
