title: Moleular models for cholecystokinin-A receptor.
abstract: Numerous techniques have been used to elucidate the structural basis for interaction of cholecystokinin (CCK)-related peptides with their hormone-binding receptor, the CCK-A receptor (CCK-AR), including structure-activity relationship studies, site-directed mutagenesis, photoaffinity-labeling, and solution NMR analysis of both CCK peptide ligands and peptide fragments derived from the CCK-A receptor. Different structural models have been developed for the peptide-receptor complexes using various subsets of the available experimental data (Giragossian & Mierke 2001; Ding et al. 2002; Escrieut et al. 2002). Here, we review details of the various models and evaluate the impact of selected experimental data sets on model development.
authors.affiliation: Department of Chemistry, Vanderbilt University, Center for Structural Biology, Nashville, TN 37235-1822, USA.
authors.forename: Eric S
authors.initials: ES
authors.lastname: Dawson
authors.forename: Randel M
authors.initials: RM
authors.lastname: Henne
authors.forename: Laurence J
authors.initials: LJ
authors.lastname: Miller
authors.forename: Terry P
authors.initials: TP
authors.lastname: Lybrand
mesh_terms: D008958:Models, Molecular; D019920:Photoaffinity Labels / Q000378:metabolism*; D011949:Receptors, Cholecystokinin / Q000737:chemistry / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D019920:Photoaffinity Labels; D011949:Receptors, Cholecystokinin