Structure of cholecystokinin receptor binding sites and mechanism of 
activation/inactivation by agonists/antagonists

Fourmy, D.; Escrieut, C.; Archer, E.; Gales, C.; Gigoux, V.; Maigret, B.; Moroder, L.; Silvente-Poirot, S.; Martinez, J.; Fehrentz, J. A.; Pradayrol, L.

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Structure of cholecystokinin receptor binding sites and mechanism of activation/inactivation by agonists/antagonists

MPS-Authors

/persons/resource/persons78419

Moroder, L.
Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Fourmy, D., Escrieut, C., Archer, E., Gales, C., Gigoux, V., Maigret, B., et al. (2002). Structure of cholecystokinin receptor binding sites and mechanism of activation/inactivation by agonists/antagonists. Pharmacology & Toxicology, 91(6), 313-320.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-6DC0-6

Abstract

Delineation of CCK receptor binding sites is a prerequisite for the understanding of the molecular basis for ligand recognition, partial agonism. ligand-induced traffiking of receptor signalling. In the current paper, we illustrate how, in the past 5 years, studies from our laboratory and others have provided new data on the molecular basis of the pharmacology and functioning of CCK1 and CCK2 receptors. Available data on CCK1 and CCK2R binding sites indicate that 1) homologous regions of the two receptors are involved in the binding site of CCK, however, positioning of CCK slightly differs; 2) binding sites of non-peptide agonists/antagonist are buried in the pocket formed by transmembrane helices and overlap that of CCK and 3) residues of the binding sites as well as of conserved motifs such as E/DRY, NPXXY are crucial for receptor activation.