Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7MIL

Mouse TRPV3 in MSP2N2 nanodiscs, sensitized state at 42 degrees Celsius

Summary for 7MIL
Entry DOI10.2210/pdb7mil/pdb
EMDB information23855
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, sensitized state at 42 degrees celsius, msp2n2, membrane protein
Biological sourceMus musculus (Mouse)
Total number of polymer chains4
Total formula weight376626.38
Authors
Nadezhdin, K.D.,Neuberger, A.,Sobolevsky, A.I. (deposition date: 2021-04-17, release date: 2021-07-21, Last modification date: 2024-10-16)
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 (3.86 Å)
Structure validation

226707

數據於2024-10-30公開中

PDB statisticsPDBj update infoContact PDBjnumon