Core Viewpoint - The research on the human sweet taste receptor reveals its unique asymmetric dimer structure and ligand recognition mechanism, providing a molecular basis for the design of new artificial sweeteners and drug development strategies targeting sweet receptors [4][9]. Group 1: Research Findings - The study published in Nature characterizes the high-resolution three-dimensional structure of the human sweet taste receptor in both apo and sucralose-bound states [4][6]. - The research team identified that sucralose binds specifically to the Venus flytrap domain of TAS1R2, highlighting the receptor's asymmetric dimer structure [7][9]. - The study utilized mutagenesis and molecular dynamics simulations to depict the recognition pattern of sweeteners within TAS1R2, revealing conformational changes and unique activation mechanisms upon ligand binding [7][9]. Group 2: Research Team and Contributions - The research was conducted by a team from ShanghaiTech University, with key contributors including researchers Huatian and Zhijie Liu, along with several doctoral and postdoctoral researchers [9]. - This study marks another breakthrough in the field of chemical sensing molecular mechanisms, following previous reports on bitter taste receptors [9].