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Default Peptide hormone binding to G-protein-coupled receptors: structural characterization v

Peptide hormone binding to G-protein-coupled receptors: structural characterization via NMR techniques.

Related Articles Peptide hormone binding to G-protein-coupled receptors: structural characterization via NMR techniques.

Med Res Rev. 2001 Sep;21(5):450-71

Authors: Mierke DF, Giragossian C

G-protein-coupled receptors (GPCRs) allow cells to respond to calcium, hormones, and neurotransmitters. Not surprisingly, they currently make up the largest family of validated drug targets. Rational drug design for molecular regulators targeting GPCRs has been limited to theoretical-based computational approaches. X-ray crystallography of intact GPCRs has provided the topological orientation of the seven transmembrane helices, but limited structural information of the extracellular and intracellular loops and protein termini. In this review we detail an NMR-based approach which provides the high-resolution structural features on the extracellular domains of GPCRs and the ligand/receptor complexes formed upon titration of the peptide hormone. The results provide important contact points and a high-resolution description of the ligand/receptor interactions, which may be useful for the rational design of therapeutic agents targeting GPCRs. Recent results from our investigation of the cholecystokinin peptide hormone system are used to highlight this approach.

PMID: 11579442 [PubMed - indexed for MEDLINE]



Source: PubMed
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