Characterization of the type A cholecystokinin receptor hormone-binding domain: Use of contrasting and complementary methodologies

Xi Qin Ding, Laurence J. Miller

Research output: Contribution to journalReview article

8 Scopus citations

Abstract

Insights into the molecular basis of binding of the peptide hormone, cholecystokinin, to its G protein-coupled receptor is of substantial interest and may contribute to the successful production and refinement of receptor-active drugs. A number of methodological approaches provide complementary data to contribute to these insights. These include receptor mutagenesis, ligand structure-activity data, conformational analysis of ligand and receptor fragments, and photoaffinity labeling. In this work, we compare and contrast each of these methods and provide our current view of the cumulative impact of the current data on molecular conformational models of the agonist-occupied type A cholecystokinin receptor. These support the key roles played by extracellular loop and tail regions of this receptor for binding its natural peptide ligand.

Original languageEnglish (US)
Pages (from-to)1223-1228
Number of pages6
JournalPeptides
Volume22
Issue number8
DOIs
StatePublished - Aug 14 2001

Keywords

  • Cholecystokinin
  • G protein-coupled receptors
  • Mutagenesis
  • Photoaffinity labeling

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience

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