Determination of ligand-receptor interactions of cholecystokinin by nuclear magnetic resonance.
To date high resolution structural studies of G protein coupled receptors, with the exception of rhodopsin, have not been feasible using conventional spectroscopic techniques. To overcome these difficulties, the structural features of partial or intact domains of GPCRs have been studied by nuclear magnetic resonance spectroscopy and X-ray crystallography. Here, we describe the structural characterization of receptor domains from the cholecystokinin 1 and 2 receptors and the elucidation of intermolecular interactions between the extracellular receptor domains and CCK-8 by solution state nmr.
Giragossian
Craig
C
Department of Chemistry, Brown University, Providence, RI 02912, USA.
Mierke
Dale F
DF
D000595:Amino Acid Sequence; D001665:Binding Sites; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D043886:Receptor, Cholecystokinin A; D043887:Receptor, Cholecystokinin B; D011949:Receptors, Cholecystokinin / Q000737:chemistry* / Q000378:metabolism
D008024:Ligands; D010446:Peptide Fragments; D043886:Receptor, Cholecystokinin A; D043887:Receptor, Cholecystokinin B; D011949:Receptors, Cholecystokinin