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 …

The presence of druggable, topographically distinct allosteric sites on a wide range of
receptor families has offered new paradigms for small molecules to modulate receptor …

Most current drugs are designed to bind directly to the primary active sites (also known as
orthosteric sites) of their biological targets. A drug binds to the active site of a biomolecule …

Allosteric interactions play vital roles in metabolic processes and signal transduction and,
more recently, have become the focus of numerous pharmacological studies because of the …

The drug discovery landscape has been transformed over the past decade by the discovery
of allosteric modulators of all major mammalian receptor superfamilies. Allosteric ligands are …

Orthosteric drugs block the active site to obstruct function; allosteric drugs modify the
population of the active state, to modulate function. Available data lead us to propose that …

Four major receptor families enable cells to respond to chemical and physical signals from
their proximal environment. The ligand-and voltage-gated ion channels, G-protein-coupled …

Currently, there are two types of drugs on the market: orthosteric, which bind at the active
site; and allosteric, which bind elsewhere on the protein surface, and allosterically change …

The question of how allostery works was posed almost 50 years ago. Since then it has been
the focus of much effort. This is for two reasons: first, the intellectual curiosity of basic science …

Many small-molecule agonists also display allosteric properties. Such ago-allosteric
modulators act as co-agonists, providing additive efficacy–instead of partial antagonism …