Nuclear magnetic resonance (NMR) analysis of ligand receptor interactions: The cholinergic system - A model

Yigal Fraenkel*, Deborah E. Shalev, Jonathan M. Gershoni, Gil Navon

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

17 Scopus citations

Abstract

Elucidation of the molecular mechanisms that govern ligand-receptor recognition is essential to the rational design of specific pharmacological reagents. Whereas often the receptor and its binding site are the target of investigation, study of the ligand in its free and bound state can also reveal important information regarding this recognition process. Nuclear magnetic resonance (NMR) spectroscopy can be extremely useful for such studies. In this review, we discuss the attributes of NMR in the study of ligand receptor interactions. The cholinergic receptor and its binding to the neurotransmitter, acetylcholine, and cholinergic antagonists serve as a model system, illustrating the power of ligand analysis by NMR. The results discussed prove that the region of residues α 180-205 of the nicotinic actylcholine receptor are an essential component of the cholinergic binding site and that ligand binding involves a positively charged hydrophobic motif.

Original languageEnglish
Pages (from-to)273-301
Number of pages29
JournalCritical Reviews in Biochemistry and Molecular Biology
Volume31
Issue number4
DOIs
StatePublished - 1996
Externally publishedYes

Keywords

  • cholinergic system
  • ligand receptor interactions
  • nuclear magnetic resonance
  • pharmacological reagents

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