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7MIM

Mouse TRPV3 in cNW11 nanodiscs, closed state at 4 degrees Celsius

Summary for 7MIM
Entry DOI10.2210/pdb7mim/pdb
EMDB information23856
DescriptorTransient receptor potential cation channel subfamily V member 3, (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate, SODIUM ION (3 entities in total)
Functional Keywordstransient receptor potential v family member 3, trp channel, trpv3, closed state at 4 degrees celsius, cnw11, membrane protein
Biological sourceMus musculus (Mouse)
Total number of polymer chains4
Total formula weight397977.48
Authors
Neuberger, A.,Nadezhdin, K.D.,Sobolevsky, A.I. (deposition date: 2021-04-17, release date: 2021-07-21, Last modification date: 2024-11-13)
Primary citationNadezhdin, K.D.,Neuberger, A.,Trofimov, Y.A.,Krylov, N.A.,Sinica, V.,Kupko, N.,Vlachova, V.,Zakharian, E.,Efremov, R.G.,Sobolevsky, A.I.
Structural mechanism of heat-induced opening of a temperature-sensitive TRP channel.
Nat.Struct.Mol.Biol., 28:564-572, 2021
Cited by
PubMed Abstract: Numerous 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.
PubMed: 34239124
DOI: 10.1038/s41594-021-00615-4
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.42 Å)
Structure validation

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