Unit

UNIT 1.22 Quantification of Allosteric Interactions at G Protein Coupled Receptors Using Radioligand Binding Assays

  1. Arthur Christopoulos

Published Online: 1 MAY 2001

DOI: 10.1002/0471141755.ph0122s11

Current Protocols in Pharmacology

Current Protocols in Pharmacology

How to Cite

Christopoulos, A. 2001. Quantification of Allosteric Interactions at G Protein Coupled Receptors Using Radioligand Binding Assays. Current Protocols in Pharmacology. 11:1.22:1.22.1–1.22.40.

Author Information

  1. University of Melbourne, Victoria, Australia

Publication History

  1. Published Online: 1 MAY 2001
  2. Published Print: DEC 2000

This is not the most recent version of the article. View current version (1 MAR 2011)

Abstract

Allosteric interactions are non-competitive in nature and involve the simultaneous binding of two ligands to the same receptor. These interactions are also commonly referred to as being cooperative. The effect of an allosteric modulator is to cause a conformational change in the receptor protein that yields a decrease or increase in the equilibrium binding affinity of a classical (orthosteric) agent, such as an agonist or competitive antagonist, for its binding site on the receptor, and vice versa. Because of the complex nature of allosteric phenomena, their detection and quantification relies on the use of both equilibrium and non-equilibrium binding assays, otherwise the phenomenon may be misinterpreted. This unit outlines the most common experimental approaches to measuring allosterism at G protein-coupled receptors, and also discusses the analysis of experimental data derived from such assays.