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.
Main Authors: | , , , , , , |
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Format: | Article |
Language: | English |
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Nature Portfolio
2021-04-01
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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. |
first_indexed | 2024-12-14T14:03:33Z |
format | Article |
id | doaj.art-c4fde09e03ba45fbaf81d692cd390f1c |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-14T14:03:33Z |
publishDate | 2021-04-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
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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