Allosteric binding sites on cell-surface receptors: novel targets for drug discovery

Nat Rev Drug Discov. 2002 Mar;1(3):198-210. doi: 10.1038/nrd746.


Cell-surface receptors are the targets for more than 60% of current drugs. Traditionally, optimizing the interaction of lead molecules with the binding site for the endogenous agonist (orthosteric site) has been viewed as the best means of achieving selectivity of action. However, recent developments have highlighted the fact that drugs can interact with binding sites on the receptor molecule that are distinct from the orthosteric site, known as allosteric sites. Allosteric modulators could offer several advantages over orthosteric ligands, including greater selectivity and saturability of their effect.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Allosteric Site
  • Animals
  • Humans
  • Kinetics
  • Pharmaceutical Preparations / chemistry
  • Receptors, Cell Surface / chemistry*
  • Receptors, Cell Surface / physiology
  • Structure-Activity Relationship


  • Pharmaceutical Preparations
  • Receptors, Cell Surface