9W0U
CryoEM structure of the T2R46 in complex with tangeretin and heterotrimeric G protein complex
This is a non-PDB format compatible entry.
Summary for 9W0U
| Entry DOI | 10.2210/pdb9w0u/pdb |
| EMDB information | 65516 |
| Descriptor | Guanine nucleotide-binding protein G(i) subunit alpha-1, 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 | g protein-coupled receptor, bitter taste receptor 14, bitter taste receptor 46, ligand binding, signal transduction, membrane protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 128993.18 |
| Authors | |
| Primary citation | Tan, Q.,Yu, Y.,Han, X.,Liu, K.,Han, S.,Wang, M.,Wei, Y.,Zhu, Y.,Chen, Q.,Ma, L.,Yi, C.,Chu, X.,Wu, B.,Zhao, Q. Ligand binding modes of the bitter taste receptor T2R14 and T2R46. Nat.Struct.Mol.Biol., 33:691-700, 2026 Cited by PubMed Abstract: Bitter taste receptors (T2Rs) are considered attractive drug targets. However, the ligand recognition and selectivity of these receptors remain elusive, hampering their drug development. Here we present seven structures of human T2R14 and T2R46 in apo or ligand-bound state. Combined with molecular docking and mutagenesis data, the structures reveal an extracellular ligand-binding site in T2R14 for most of its ligands, which is different from the intracellular binding site reported recently. In contrast, T2R46 exhibits a conserved binding pocket that accommodates various ligands with distinct interaction patterns. Furthermore, the second extracellular loop in T2R14 and T2R46 acts as a tethered agonist to potentially facilitate agonist response of these two receptors to the weak tastant agonists. These findings could accelerate drug discovery targeting T2Rs. PubMed: 42009775DOI: 10.1038/s41594-026-01786-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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