Structural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channel

Structural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channel

Hetero-oligomeric TRP-like channels such as PKD1L3/PKD2L1 play crucial roles in a range of physiological and pathophysiological processes. Here, the authors present the cryo-EM structures of a minimal functional murine PKD1L3/PKD2L1 complex in the absence and presence of calcium and further supporte...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Qiang Su, Mengying Chen, Yan Wang, Bin Li, Dan Jing, Xiechao Zhan, Yong Yu, Yigong Shi
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
Materias:
Science
Q
Acceso en línea:https://doaj.org/article/a58b79945a0d42c5b08a86652fb5596b
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:a58b79945a0d42c5b08a86652fb5596b
record_format dspace
spelling oai:doaj.org-article:a58b79945a0d42c5b08a86652fb5596b2021-12-02T18:50:44ZStructural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channel10.1038/s41467-021-25216-z2041-1723https://doaj.org/article/a58b79945a0d42c5b08a86652fb5596b2021-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25216-zhttps://doaj.org/toc/2041-1723Hetero-oligomeric TRP-like channels such as PKD1L3/PKD2L1 play crucial roles in a range of physiological and pathophysiological processes. Here, the authors present the cryo-EM structures of a minimal functional murine PKD1L3/PKD2L1 complex in the absence and presence of calcium and further supported through structure-guided mutagenic studies, they discuss the mechanism of calcium-induced channel activation.Qiang SuMengying ChenYan WangBin LiDan JingXiechao ZhanYong YuYigong ShiNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Qiang Su
Mengying Chen
Yan Wang
Bin Li
Dan Jing
Xiechao Zhan
Yong Yu
Yigong Shi
Structural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channel
description Hetero-oligomeric TRP-like channels such as PKD1L3/PKD2L1 play crucial roles in a range of physiological and pathophysiological processes. Here, the authors present the cryo-EM structures of a minimal functional murine PKD1L3/PKD2L1 complex in the absence and presence of calcium and further supported through structure-guided mutagenic studies, they discuss the mechanism of calcium-induced channel activation.
format article
author Qiang Su
Mengying Chen
Yan Wang
Bin Li
Dan Jing
Xiechao Zhan
Yong Yu
Yigong Shi
author_facet Qiang Su
Mengying Chen
Yan Wang
Bin Li
Dan Jing
Xiechao Zhan
Yong Yu
Yigong Shi
author_sort Qiang Su
title Structural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channel
title_short Structural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channel
title_full Structural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channel
title_fullStr Structural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channel
title_full_unstemmed Structural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channel
title_sort structural basis for ca2+ activation of the heteromeric pkd1l3/pkd2l1 channel
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/a58b79945a0d42c5b08a86652fb5596b
work_keys_str_mv AT qiangsu structuralbasisforca2activationoftheheteromericpkd1l3pkd2l1channel
AT mengyingchen structuralbasisforca2activationoftheheteromericpkd1l3pkd2l1channel
AT yanwang structuralbasisforca2activationoftheheteromericpkd1l3pkd2l1channel
AT binli structuralbasisforca2activationoftheheteromericpkd1l3pkd2l1channel
AT danjing structuralbasisforca2activationoftheheteromericpkd1l3pkd2l1channel
AT xiechaozhan structuralbasisforca2activationoftheheteromericpkd1l3pkd2l1channel
AT yongyu structuralbasisforca2activationoftheheteromericpkd1l3pkd2l1channel
AT yigongshi structuralbasisforca2activationoftheheteromericpkd1l3pkd2l1channel
_version_ 1718377523052544000

Ejemplares similares