Structure of the cold- and menthol-sensing ion channel TRPM8.
Journal Article (Journal Article)
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.
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Duke Authors
Cited Authors
- Yin, Y; Wu, M; Zubcevic, L; Borschel, WF; Lander, GC; Lee, S-Y
Published Date
- January 12, 2018
Published In
Volume / Issue
- 359 / 6372
Start / End Page
- 237 - 241
PubMed ID
- 29217583
Pubmed Central ID
- PMC5810135
Electronic International Standard Serial Number (EISSN)
- 1095-9203
Digital Object Identifier (DOI)
- 10.1126/science.aan4325
Language
- eng
Conference Location
- United States