Author
Listed:
- Nipawan Nuemket
(Laboratory of Structural Biology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
RIKEN SPring-8 Center
Present address: Protein Crystal Analysis Division, Japan Synchrotron Radiation Research Institute, 1-1-1, Kouto, Sayo 679-5198, Japan)
- Norihisa Yasui
(Laboratory of Structural Biology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University)
- Yuko Kusakabe
(Food Research Institute, NARO)
- Yukiyo Nomura
(Laboratory of Structural Biology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University)
- Nanako Atsumi
(Laboratory of Structural Biology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University)
- Shuji Akiyama
(Research Center of Integrative Molecular System (CIMoS), Institute for Molecular Science, National Institute of Natural Sciences
The Graduate University for Advanced Studies (SOKENDAI))
- Eriko Nango
(RIKEN SPring-8 Center)
- Yukinari Kato
(New Industry Creation Hatchery Center, Tohoku University
Tohoku University Graduate School of Medicine)
- Mika K. Kaneko
(Tohoku University Graduate School of Medicine)
- Junichi Takagi
(Institute for Protein Research, Osaka University)
- Maiko Hosotani
(Laboratory of Structural Biology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University)
- Atsuko Yamashita
(Laboratory of Structural Biology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
RIKEN SPring-8 Center)
Abstract
The taste receptor type 1 (T1r) family perceives ‘palatable’ tastes. These receptors function as T1r2-T1r3 and T1r1-T1r3 heterodimers to recognize a wide array of sweet and umami (savory) tastes in sugars and amino acids. Nonetheless, it is unclear how diverse tastes are recognized by so few receptors. Here we present crystal structures of the extracellular ligand-binding domains (LBDs), the taste recognition regions of the fish T1r2-T1r3 heterodimer, bound to different amino acids. The ligand-binding pocket in T1r2LBD is rich in aromatic residues, spacious and accommodates hydrated percepts. Biophysical studies show that this binding site is characterized by a broad yet discriminating chemical recognition, contributing for the particular trait of taste perception. In contrast, the analogous pocket in T1r3LBD is occupied by a rather loosely bound amino acid, suggesting that the T1r3 has an auxiliary role. Overall, we provide a structural basis for understanding the chemical perception of taste receptors.
Suggested Citation
Nipawan Nuemket & Norihisa Yasui & Yuko Kusakabe & Yukiyo Nomura & Nanako Atsumi & Shuji Akiyama & Eriko Nango & Yukinari Kato & Mika K. Kaneko & Junichi Takagi & Maiko Hosotani & Atsuko Yamashita, 2017.
"Structural basis for perception of diverse chemical substances by T1r taste receptors,"
Nature Communications, Nature, vol. 8(1), pages 1-10, August.
Handle:
RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15530
DOI: 10.1038/ncomms15530
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Cited by:
- Kento Ojima & Wataru Kakegawa & Tokiwa Yamasaki & Yuta Miura & Masayuki Itoh & Yukiko Michibata & Ryou Kubota & Tomohiro Doura & Eriko Miura & Hiroshi Nonaka & Seiya Mizuno & Satoru Takahashi & Michis, 2022.
"Coordination chemogenetics for activation of GPCR-type glutamate receptors in brain tissue,"
Nature Communications, Nature, vol. 13(1), pages 1-17, December.
- Michael R. Schamber & Reza Vafabakhsh, 2022.
"Mechanism of sensitivity modulation in the calcium-sensing receptor via electrostatic tuning,"
Nature Communications, Nature, vol. 13(1), pages 1-14, December.
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