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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

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • 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