UNIT 1.22 Quantification of Allosteric Interactions at G Protein Coupled Receptors Using Radioligand Binding Assays
Published Online: 1 MAY 2001
Copyright © 2003 by John Wiley and Sons, Inc.
Lab Protocol Title
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.
- Published Online: 1 MAY 2001
- Published Print: DEC 2000
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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.