Structure of the cold- And menthol-sensing ion channel TRPM8
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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.
Published Version (Please cite this version)10.1126/science.aan4325
Publication InfoBorschel, WF; Lander, GC; Lee, SY; Wu, M; Yin, Ying; & Zubcevic, L (2018). Structure of the cold- And menthol-sensing ion channel TRPM8. Science, 359(6372). pp. 237-241. 10.1126/science.aan4325. Retrieved from https://hdl.handle.net/10161/16015.
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