2025 年 24 巻 3 号 p. 74-76
Molecular dynamics simulations were performed on the ligand-bound taste receptor proteins T1r2a-T1r3, followed by principal component analysis (PCA). PCA confirmed that ligand binding induces opening and closing motion of the lower part of the protein (the part closer to the cell membrane), with significant movement particularly in T1r3. The free energy landscape revealed features of metastable states reflecting this movement. These results suggest that the movement of T1r3 induced by ligand binding may play an important role in triggering signal transmission to the transmembrane region of the taste receptor.
