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9NOX

Transmembrane domains of the human TAS1R2 sweet receptor subunit in complex with miniGs/gust25

9NOX の概要
エントリーDOI10.2210/pdb9nox/pdb
EMDBエントリー49620
分子名称miniGs/gust25, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, ... (5 entities in total)
機能のキーワードsweet, taste, receptor, gpcr, tas1r2, tas1r3, t1r2, t1r3, membrane protein
由来する生物種Homo sapiens
詳細
タンパク質・核酸の鎖数5
化学式量合計283338.92
構造登録者
Juen, Z.,Lu, Z.,Yu, R.,Chang, A.N.,Wang, B.,Fitzpatrick, A.W.P.,Zuker, C.S. (登録日: 2025-03-10, 公開日: 2025-05-14, 最終更新日: 2025-08-06)
主引用文献Juen, Z.,Lu, Z.,Yu, R.,Chang, A.N.,Wang, B.,Fitzpatrick, A.W.P.,Zuker, C.S.
The structure of human sweetness.
Cell, 188:4141-4153.e18, 2025
Cited by
PubMed Abstract: In humans, the detection and ultimately the perception of sweetness begin in the oral cavity, where taste receptor cells (TRCs) dedicated to sweet-sensing interact with sugars, artificial sweeteners, and other sweet-tasting chemicals. Human sweet TRCs express on their cell surface a sweet receptor that initiates the cascade of signaling events responsible for our strong attraction to sweet stimuli. Here, we describe the cryo-electron microscopy (cryo-EM) structure of the human sweet receptor bound to two of the most widely used artificial sweeteners-sucralose and aspartame. Our results reveal the structural basis for sweet detection, provide insights into how a single receptor mediates all our responses to such a wide range of sweet-tasting compounds, and open up unique possibilities for designing a generation of taste modulators informed by the structure of the human receptor.
PubMed: 40339580
DOI: 10.1016/j.cell.2025.04.021
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3 Å)
構造検証レポート
Validation report summary of 9nox
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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