5X2M

Crystal structure of the medaka fish taste receptor T1r2a-T1r3 ligand binding domains in complex with L-glutamine

5X2M の概要

• エントリーDOI: 10.2210/pdb5x2m/pdb
• 関連するPDBエントリー: 5X2N 5X2O 5X2P 5X2Q
• 分子名称: Taste receptor, type 1, member 2a, Taste receptor, type 1, member 3, Fab16A Heavy chain, ... (10 entities in total)
• 機能のキーワード: receptor, ligand binding, amino acid, venus-flytrap domain, signaling protein-immune system complex, signaling protein/immune system
• 由来する生物種: Oryzias latipes (Japanese rice fish); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 312106.20

構造登録者

Nuemket, N.,Yasui, N.,Atsumi, N.,Yamashita, A. (登録日: 2017-02-02, 公開日: 2017-05-24, 最終更新日: 2024-10-23)

主引用文献

Nuemket, N.,Yasui, N.,Kusakabe, Y.,Nomura, Y.,Atsumi, N.,Akiyama, S.,Nango, E.,Kato, Y.,Kaneko, M.K.,Takagi, J.,Hosotani, M.,Yamashita, A.
Structural basis for perception of diverse chemical substances by T1r taste receptors
Nat Commun, 8:15530-15530, 2017

PubMed 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.

PubMed: 28534491
DOI: 10.1038/ncomms15530

実験手法

X-RAY DIFFRACTION (2.206 Å)