Allosteric enhancers, allosteric agonists and ago-allosteric modulators: where do they bind and how do they act?

Research output: Contribution to journalJournal articleResearchpeer-review

Many small-molecule agonists also display allosteric properties. Such ago-allosteric modulators act as co-agonists, providing additive efficacy--instead of partial antagonism--and they can affect--and often improve--the potency of the endogenous agonist. Surprisingly, the apparent binding sites of several ordinary allosteric enhancers and ago-allosteric modulators seem to overlap with those of the endogenous agonists. Different molecular scenarios are proposed to explain this discrepancy from classical allosteric models. In one scenario, the ago-allosteric modulator can interchange between different binding modes. In another, dimeric, receptor scenario, the endogenous agonist binds to one protomer while the ago-allosteric modulator binds to the other, 'allosteric' protomer. It is suggested that testing for ago-allosteric properties should be an integral part of the agonist drug discovery process because a compound that acts with--rather than against--the endogenous agonist could be an optimal agonist drug.
Original languageEnglish
JournalTIPS - Trends in Pharmacological Sciences
Volume28
Issue number8
Pages (from-to)366-73
Number of pages7
ISSN0165-6147
DOIs
Publication statusPublished - 2007

Bibliographical note

Keywords: Allosteric Regulation; Binding Sites; Humans; Ligands; Models, Biological; Pharmaceutical Preparations; Protein Binding; Receptors, GABA; gamma-Aminobutyric Acid

ID: 10149982