9O38

Transmembrane domains of the human sweet receptor (TAS1R2 + TAS1R3) from Class 3 particles (rigidly fitted from PDB:9NOX and 9NOR)

Summary for 9O38

• Entry DOI: 10.2210/pdb9o38/pdb
• Related: 9NOR 9NOX
• EMDB information: 70072
• Descriptor: Taste receptor type 1 member 3,Guanine nucleotide-binding protein G(s) subunit alpha isoforms short, 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)
• Functional Keywords: sweet, taste, receptor, gpcr, tas1r2, tas1r3, t1r2, t1r3, hydrolase-immune system complex, human, hydrolase/immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 6
• Total formula weight: 407808.25

Authors

Juen, Z.,Lu, Z.,Yu, R.,Chang, A.N.,Wang, B.,Fitzpatrick, A.W.P.,Zuker, C.S. (deposition date: 2025-04-06, release date: 2025-05-14, Last modification date: 2025-05-21)

Primary citation

Juen, Z.,Lu, Z.,Yu, R.,Chang, A.N.,Wang, B.,Fitzpatrick, A.W.P.,Zuker, C.S.
The structure of human sweetness.
Cell, 2025

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

Experimental method

ELECTRON MICROSCOPY (3 Å)