Extracellular cap domain is an essential component of the TRPV1 gating mechanism

Structural and functional characterization of the full-length TRPV1 channel from the thirteen-lined ground squirrel reveal the architecture of the extracellular cap domain and the intracellular C-terminus, and suggest a role of the cap domain in TRPV1 conductance and ion selectivity.

Bibliographic Details
Main Authors: Kirill D. Nadezhdin, Arthur Neuberger, Yury A. Nikolaev, Lyle A. Murphy, Elena O. Gracheva, Sviatoslav N. Bagriantsev, Alexander I. Sobolevsky
Format: Article
Language:English
Published: Nature Portfolio 2021-04-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-22507-3
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author Kirill D. Nadezhdin
Arthur Neuberger
Yury A. Nikolaev
Lyle A. Murphy
Elena O. Gracheva
Sviatoslav N. Bagriantsev
Alexander I. Sobolevsky
author_facet Kirill D. Nadezhdin
Arthur Neuberger
Yury A. Nikolaev
Lyle A. Murphy
Elena O. Gracheva
Sviatoslav N. Bagriantsev
Alexander I. Sobolevsky
author_sort Kirill D. Nadezhdin
collection DOAJ
description Structural and functional characterization of the full-length TRPV1 channel from the thirteen-lined ground squirrel reveal the architecture of the extracellular cap domain and the intracellular C-terminus, and suggest a role of the cap domain in TRPV1 conductance and ion selectivity.
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spelling doaj.art-c4fde09e03ba45fbaf81d692cd390f1c2022-12-21T22:58:39ZengNature PortfolioNature Communications2041-17232021-04-011211810.1038/s41467-021-22507-3Extracellular cap domain is an essential component of the TRPV1 gating mechanismKirill D. Nadezhdin0Arthur Neuberger1Yury A. Nikolaev2Lyle A. Murphy3Elena O. Gracheva4Sviatoslav N. Bagriantsev5Alexander I. Sobolevsky6Department of Biochemistry and Molecular Biophysics, Columbia UniversityDepartment of Biochemistry and Molecular Biophysics, Columbia UniversityDepartment of Cellular and Molecular Physiology, Yale University School of MedicineDepartment of Cellular and Molecular Physiology, Yale University School of MedicineDepartment of Cellular and Molecular Physiology, Yale University School of MedicineDepartment of Cellular and Molecular Physiology, Yale University School of MedicineDepartment of Biochemistry and Molecular Biophysics, Columbia UniversityStructural and functional characterization of the full-length TRPV1 channel from the thirteen-lined ground squirrel reveal the architecture of the extracellular cap domain and the intracellular C-terminus, and suggest a role of the cap domain in TRPV1 conductance and ion selectivity.https://doi.org/10.1038/s41467-021-22507-3
spellingShingle Kirill D. Nadezhdin
Arthur Neuberger
Yury A. Nikolaev
Lyle A. Murphy
Elena O. Gracheva
Sviatoslav N. Bagriantsev
Alexander I. Sobolevsky
Extracellular cap domain is an essential component of the TRPV1 gating mechanism
Nature Communications
title Extracellular cap domain is an essential component of the TRPV1 gating mechanism
title_full Extracellular cap domain is an essential component of the TRPV1 gating mechanism
title_fullStr Extracellular cap domain is an essential component of the TRPV1 gating mechanism
title_full_unstemmed Extracellular cap domain is an essential component of the TRPV1 gating mechanism
title_short Extracellular cap domain is an essential component of the TRPV1 gating mechanism
title_sort extracellular cap domain is an essential component of the trpv1 gating mechanism
url https://doi.org/10.1038/s41467-021-22507-3
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