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Researchers at the Center for Genomic Regulation (CRG) have developed a new way of identifying new druggable sites on a family of proteins that could help design treatments with fewer side effects for a very wide range of conditions from heart disease to depression.

The method allows scientists to create detailed functional maps of G protein-coupled receptors, or GPCRs, a type of protein that sits on the surface of a cell. One in three regulator-approved drugs worldwide targets this family of proteins.

There are 800 different types of GPCRs. Adrenaline, histamine and serotonin all rely on different variants to transmit signals from the outside world into the cell. They are also targets for beta blockers, antihistamines, opioids and asthma inhalers.

However, each GPCR's architecture is similar enough that a drug designed to hit one target often hits others too, causing unintended and unwanted side effects. Designing a drug that reliably prefers one over the other has been largely a matter of luck.

A study led by Taylor Mighell and Ben Lehner and published in Nature Structural & Molecular Biology shows a new way of building a map of the beta-2 adrenergic receptor, a GPCR that tells cells to relax airways. It is a drug target for asthma and COPD inhalers such as salbutamol and salmeterol.

They built it by creating thousands of variants of the protein, swapping one building block for another.

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