Interaction of sweet proteins with their receptor. A conformational study of peptides corresponding to loops of brazzein, monellin and thaumatin.

@article{Tancredi2004InteractionOS,
  title={Interaction of sweet proteins with their receptor. A conformational study of peptides corresponding to loops of brazzein, monellin and thaumatin.},
  author={Teodorico Tancredi and Annalisa Pastore and Severo Salvadori and Veronica Esposito and Piero Andrea Temussi},
  journal={European journal of biochemistry},
  year={2004},
  volume={271 11},
  pages={2231-40}
}
The mechanism of interaction of sweet proteins with the T1R2-T1R3 sweet taste receptor has not yet been elucidated. Low molecular mass sweeteners and sweet proteins interact with the same receptor, the human T1R2-T1R3 receptor. The presence on the surface of the proteins of "sweet fingers", i.e. protruding features with chemical groups similar to those of low molecular mass sweeteners that can probe the active site of the receptor, would be consistent with a single mechanism for the two classes… CONTINUE READING