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...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2021-08-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-021-25216-z |
| _version_ | 1818419927523000320 |
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| 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 |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-14T12:46:21Z |
| format | Article |
| id | doaj.art-a58b79945a0d42c5b08a86652fb5596b |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-14T12:46:21Z |
| publishDate | 2021-08-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-a58b79945a0d42c5b08a86652fb5596b2022-12-21T23:00:45ZengNature PortfolioNature Communications2041-17232021-08-0112111010.1038/s41467-021-25216-zStructural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channelQiang Su0Mengying Chen1Yan Wang2Bin Li3Dan Jing4Xiechao Zhan5Yong Yu6Yigong Shi7Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake UniversityBeijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, School of Medicine, Tsinghua UniversityDepartment of Biological Sciences, St. John’s UniversityDepartment of Biological Sciences, St. John’s UniversityKey Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake UniversityKey Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake UniversityDepartment of Biological Sciences, St. John’s UniversityKey Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake UniversityHetero-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.https://doi.org/10.1038/s41467-021-25216-z |
| spellingShingle | 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 Nature Communications |
| title | 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_short | Structural basis for Ca2+ activation of the heteromeric PKD1L3/PKD2L1 channel |
| title_sort | structural basis for ca2 activation of the heteromeric pkd1l3 pkd2l1 channel |
| url | https://doi.org/10.1038/s41467-021-25216-z |
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