Structural mechanism of heat-induced opening of a temperature-sensitive TRP channel
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F21%3A00544567" target="_blank" >RIV/67985823:_____/21:00544567 - isvavai.cz</a>
Result on the web
<a href="https://doi.org/10.1038/s41594-021-00615-4" target="_blank" >https://doi.org/10.1038/s41594-021-00615-4</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41594-021-00615-4" target="_blank" >10.1038/s41594-021-00615-4</a>
Alternative languages
Result language
angličtina
Original language name
Structural mechanism of heat-induced opening of a temperature-sensitive TRP channel
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
30103 - Neurosciences (including psychophysiology)
Result continuities
Project
<a href="/en/project/GA19-03777S" target="_blank" >GA19-03777S: Molecular Basis of Thermosensitive TRP Ion Channel Regulation in Nociceptive Neurons</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Nature Structural & Molecular Biology
ISSN
1545-9993
e-ISSN
1545-9985
Volume of the periodical
28
Issue of the periodical within the volume
7
Country of publishing house
US - UNITED STATES
Number of pages
9
Pages from-to
564-572
UT code for WoS article
000670865500003
EID of the result in the Scopus database
2-s2.0-85109966115