Structural highlights
Publication Abstract from PubMed
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 A. 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.
Structure of the cold- and menthol-sensing ion channel TRPM8.,Yin Y, Wu M, Zubcevic L, Borschel WF, Lander GC, Lee SY Science. 2017 Dec 7. pii: science.aan4325. doi: 10.1126/science.aan4325. PMID:29217583[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yin Y, Wu M, Zubcevic L, Borschel WF, Lander GC, Lee SY. Structure of the cold- and menthol-sensing ion channel TRPM8. Science. 2017 Dec 7. pii: science.aan4325. doi: 10.1126/science.aan4325. PMID:29217583 doi:http://dx.doi.org/10.1126/science.aan4325