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TitleStructure of the cold- and menthol-sensing ion channel TRPM8.
Journal, issue, pagesScience, Vol. 359, Issue 6372, Page 237-241, Year 2018
Publish dateJan 12, 2018
AuthorsYing Yin / Mengyu Wu / Lejla Zubcevic / William F Borschel / Gabriel C Lander / Seok-Yong Lee /
PubMed AbstractTransient 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 ...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.
External linksScience / PubMed:29217583 / PubMed Central
MethodsEM (single particle)
Resolution4.1 Å
Structure data

7127

6bpq

EMDB-7127, PDB-6bpq:
Structure of the cold- and menthol-sensing ion channel TRPM8
Method: EM (single particle) / Resolution: 4.1 Å

Source
  • ficedula albicollis (Collared flycatcher)
KeywordsTRANSPORT PROTEIN / cold sensor / menthol sensor / calcium-permeable ion channel / ion channel

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