Paper published in PNAS
Glad to share our latest work in PNAS
Our study reveals the underlying molecular mechanisms of ligand-induced activation in the human bitter taste receptor TAS2R5. Despite similar binding energies, significant variations in agonist potencies were observed. Using live cell-based assays, optical resonators, and molecular dynamics simulations, we found that the activation energy of the opening of the Gα subunit for GDP–GTP exchange, rather than binding affinity alone, correlates highly with agonist potency. This finding refines our understanding of G protein-coupled receptor (GPCR) activation, paving the way for the rational design of new therapeutic agents targeting these receptors.