Journal
SCIENCE
Volume 359, Issue 6372, Pages 237-241Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aan4325
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Funding
- National Institutes of Health [R35NS097241, DP2EB020402]
- NIH [S10OD021634]
- Protein Data Bank [6BPQ]
- EMDB [EMD-7127]
- NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING [DP2EB020402] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [R35NS097241] Funding Source: NIH RePORTER
- OFFICE OF THE DIRECTOR, NATIONAL INSTITUTES OF HEALTH [S10OD021634] Funding Source: NIH RePORTER
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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 similar to 4.1 angstroms. 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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