The article presents a detailed examination of the human sweet taste receptor (TAS1R2-TAS1R3) utilizing cryo-electron microscopy, revealing its structure in both unbound and sucralose-bound forms. It highlights the receptor's asymmetric heterodimer architecture and specifies that sucralose binds solely at the Venus flytrap domain of TAS1R2. Through mutagenesis and molecular dynamics simulations, the study clarifies sweetener recognition modes, structural conformations induced by ligand binding, and unique activation methods. These findings significantly enhance our understanding of chemosensory receptor functioning and could inform the development of next-generation sweeteners affecting metabolic health and dietary choices.
The cryo-EM structures of the human sweet taste receptor provide insights into the receptor's architecture and its unique activation mechanism upon ligand binding.
Our study delineates how sweeteners are recognized within the TAS1R2 receptor, offering a molecular basis for designing new sweeteners that influence taste perception.
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