6BPQ
Structure of the cold- and menthol-sensing ion channel TRPM8
Summary for 6BPQ
| Entry DOI | 10.2210/pdb6bpq/pdb |
| EMDB information | 7127 |
| Descriptor | Transient receptor potential cation channel subfamily M member 8 (1 entity in total) |
| Functional Keywords | cold sensor, menthol sensor, calcium-permeable ion channel, ion channel, transport protein |
| Biological source | Ficedula albicollis (Collared flycatcher) |
| Total number of polymer chains | 4 |
| Total formula weight | 431381.12 |
| Authors | Yin, Y.,Wu, M.,Zubcevic, L.,Borschel, W.F.,Lander, G.C.,Lee, S.-Y. (deposition date: 2017-11-25, release date: 2017-12-13, Last modification date: 2024-03-13) |
| Primary citation | Yin, Y.,Wu, M.,Zubcevic, L.,Borschel, W.F.,Lander, G.C.,Lee, S.Y. Structure of the cold- and menthol-sensing ion channel TRPM8. Science, 359:237-241, 2018 Cited by PubMed Abstract: Transient receptor potential melastatin (TRPM) cation channels are polymodal sensors that are involved in a variety of physiological processes. Within the TRPM family, member 8 (TRPM8) is the primary cold and menthol sensor in humans. We determined the cryo-electron microscopy structure of the full-length TRPM8 from the collared flycatcher at an overall resolution of ~4.1 ångstroms. Our TRPM8 structure reveals a three-layered architecture. The amino-terminal domain with a fold distinct among known TRP structures, together with the carboxyl-terminal region, forms a large two-layered cytosolic ring that extensively interacts with the transmembrane channel layer. The structure suggests that the menthol-binding site is located within the voltage-sensor-like domain and thus provides a structural glimpse of the design principle of the molecular transducer for cold and menthol sensation. PubMed: 29217583DOI: 10.1126/science.aan4325 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.1 Å) |
Structure validation
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