Počet záznamů: 1
Structural mechanism of heat-induced opening of a temperature-sensitive TRP channel
- 1.
SYSNO ASEP 0544567 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Structural mechanism of heat-induced opening of a temperature-sensitive TRP channel Tvůrce(i) Nadezhdin, K. D. (US)
Neuberger, A. (US)
Trofimov, Yu. A. (RU)
Krylov, N. A. (RU)
Sinica, Viktor (FGU-C) RID, ORCID, SAI
Kupko, N. (US)
Vlachová, Viktorie (FGU-C) RID, ORCID, SAI
Zakharian, E. (US)
Efremov, R. G. (RU)
Sobolevsky, A. I. (US)Zdroj.dok. Nature Structural & Molecular Biology. - : Nature Publishing Group - ISSN 1545-9993
Roč. 28, č. 7 (2021), s. 564-572Poč.str. 9 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova temperature sensitive TRP channel ; gating ; heat-activated channel ; structure-function ; vanilloid TRP channel Vědní obor RIV FH - Neurologie, neurochirurgie, neurovědy Obor OECD Neurosciences (including psychophysiology CEP GA19-03777S GA ČR - Grantová agentura ČR Způsob publikování Omezený přístup Institucionální podpora FGU-C - RVO:67985823 UT WOS 000670865500003 EID SCOPUS 85109966115 DOI 10.1038/s41594-021-00615-4 Anotace 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. Pracoviště Fyziologický ústav Kontakt Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400 Rok sběru 2022 Elektronická adresa https://doi.org/10.1038/s41594-021-00615-4
Počet záznamů: 1