Abstract
The umami taste receptor is a heterodimer composed of two members of the T1R taste receptor family: T1R1 and T1R3. The homology models of the ligand binding domains of the human umami receptor have been constructed based on crystallographic structures of the taste receptor of the central nervous system. Furthermore, the molecular simulations of the ligand binding domain show that the likely conformation was that T1R1 protein exists in the closed conformation, and T1R3 in the open conformation in the heterodimer. The molecular docking study of T1R1 and T1R3 in complex with four peptides, including Lys–Gly–Asp–Glu–Ser–Leu–Leu–Ala, Ser–Glu–Glu, G1u–Ser, and Asp–Glu–Ser, displayed that the amino acid residue of SER146 and Glu277 in T1R3 may play great roles in the synergism of umami taste. This docking result further validated the robustness of the model. In the paper, binding of umami peptide and the T1R1/T1R3 receptor was first described and the interaction is the base of umami activity theory.
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Acknowledgments
This work was supported by the National Natural Science Foundation of China under Grant No. 31101344, by Health Bureau of Zhejiang Province under Grant No. 2011KYB002 and the Fundamental Research Funds for the Central Universities (XDJK2010C015).
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Dang, Y., Gao, X., Xie, A. et al. Interaction Between Umami Peptide and Taste Receptor T1R1/T1R3. Cell Biochem Biophys 70, 1841–1848 (2014). https://doi.org/10.1007/s12013-014-0141-z
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DOI: https://doi.org/10.1007/s12013-014-0141-z