Structural highlights
Publication Abstract from PubMedNumerous physiological functions rely on distinguishing temperature through temperature-sensitive transient receptor potential channels (thermo-TRPs). Although the function of thermo-TRPs has been studied extensively, structural determination of their heat- and cold-activated states has remained a challenge. Here, we present cryo-EM structures of the nanodisc-reconstituted wild-type mouse TRPV3 in three distinct conformations: closed, heat-activated sensitized and open states. The heat-induced transformations of TRPV3 are accompanied by changes in the secondary structure of the S2-S3 linker and the N and C termini and represent a conformational wave that links these parts of the protein to a lipid occupying the vanilloid binding site. State-dependent differences in the behavior of bound lipids suggest their active role in thermo-TRP temperature-dependent gating. Our structural data, supported by physiological recordings and molecular dynamics simulations, provide an insight for understanding the molecular mechanism of temperature sensing. Structural mechanism of heat-induced opening of a temperature-sensitive TRP channel.,Nadezhdin KD, Neuberger A, Trofimov YA, Krylov NA, Sinica V, Kupko N, Vlachova V, Zakharian E, Efremov RG, Sobolevsky AI Nat Struct Mol Biol. 2021 Jul;28(7):564-572. doi: 10.1038/s41594-021-00615-4., Epub 2021 Jul 8. PMID:34239124[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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