Trends

Allosteric binding sites are pockets that small molecules can interact with outside the orthosteric pocket used by the natural signalling molecule (agonist).

Although they were long understood to exist and be important for G protein-coupled receptors (GPCRs), the range and diversity of these allosteric pockets was not predicted, with sites buried deep inside the proteins, lodged on the side within the cell membrane, and inside the cell disrupting G protein binding.

The diversity of both the pockets themselves and how molecules modulate the function of GPCRs gives great potential for future structure-based drug design for GPCRs.