Taste-modifying Sweet Protein, Neoculin, is Received at Human T1r3 Amino Terminal Domain.
From: Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Tokyo, Japan.
Biochemical and biophysical research communications
- Publish Date: Jun 2007
- ISSN: 0006-291X
- Volume: 358
- Issue: 2
- Pages: 585-9
- Medium: Print
- Language: English
- Citation (JAMA): Koizumi Ayako, Nakajima Ken-ichiro, Asakura Tomiko, et al. Taste-modifying Sweet Protein, Neoculin, is Received at Human T1r3 Amino Terminal Domain.. Biochem. Biophys. Res. Commun. Jun 2007;358:585-9
Abstract
This study examines taste reception of neoculin, a Curculigo latifolia sweet protein with taste-modifying activity which converts sourness to sweetness. Neoculin tastes sweet to humans, but not to mice, and is received by the human sweet taste receptor hT1R2-hT1R3. In the present study with calcium imaging analysis of HEK cells expressing human and mouse T1Rs, we demonstrated that hT1R3 is required for the reception of neoculin. Further experiments using human/mouse chimeric T1R3s revealed that the extracellular amino terminal domain (ATD) of hT1R3 is essential for the reception of neoculin. Although T1R2-T1R3 is known to have multiple potential ligand-binding sites to receive a wide variety of sweeteners, the present study is apparently the first to identify the ATD of hT1R3 as a new sweetener-binding region.
Mesh Headings (Keywords): Amino Acid Sequence, Binding Sites, Cell Line, Humans, Kidney, Molecular Sequence Data, Plant Proteins, Protein Binding, Receptors, G-Protein-Coupled, Sweetening Agents
Check for Full Text / PubMed Unique Identifier (PMID): 17499612
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