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Researchers found that when bitter tastants come into contact with TAS2R14 receptors, the chemicals wedge themselves into to a specific spot on the receptor called an allosteric site, this causes the protein to change its shape, activating the attached G protein.

"Cholesterol was residing in another binding site called the orthosteric pocket in TAS2R14, while the bitter tastant binds to the allosteric site," said Kim.

The allosteric binding region is located between TAS2R14 and its coupled G protein is called G-protein alpha.

"In the future, this structure will be key to discovering and designing drug candidates that can directly regulate G proteins through the allosteric sites," said Kim.

The discovery of this novel allosteric binding site for bitter tasting substances is unique.