Cryo-EM structure of the polycystin 2-l1 ion channel
We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel. Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes. The related primary cilium-specific polycystin...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2018-07-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/36931 |
| _version_ | 1828380183049011200 |
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| author | Raymond E Hulse Zongli Li Rick K Huang Jin Zhang David E Clapham |
| author_facet | Raymond E Hulse Zongli Li Rick K Huang Jin Zhang David E Clapham |
| author_sort | Raymond E Hulse |
| collection | DOAJ |
| description | We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel. Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes. The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics. Here we show that these differences are reflected in the architecture of polycystin 2-l1. |
| first_indexed | 2024-12-10T03:52:20Z |
| format | Article |
| id | doaj.art-4fba5978103d4fb8a50805315ff8f96b |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-12-10T03:52:20Z |
| publishDate | 2018-07-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-4fba5978103d4fb8a50805315ff8f96b2022-12-22T02:03:13ZengeLife Sciences Publications LtdeLife2050-084X2018-07-01710.7554/eLife.36931Cryo-EM structure of the polycystin 2-l1 ion channelRaymond E Hulse0https://orcid.org/0000-0002-0110-3752Zongli Li1Rick K Huang2Jin Zhang3David E Clapham4https://orcid.org/0000-0002-4459-9428Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States; Department of Cardiology, Howard Hughes Medical Institute, Boston Children’s Hospital, Boston, United StatesDepartment of Biological Chemistry and Molecular Pharmacology, Howard Hughes Medical Institute, Harvard Medical School, Boston, United StatesJanelia Research Campus, Howard Hughes Medical Institute, Ashburn, United StatesJanelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States; School of Basic Medical Sciences, Nanchang University, Nanchang, ChinaJanelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States; Department of Cardiology, Howard Hughes Medical Institute, Boston Children’s Hospital, Boston, United StatesWe report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel. Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes. The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics. Here we show that these differences are reflected in the architecture of polycystin 2-l1.https://elifesciences.org/articles/36931PC-2L1calciumTRP channelcryo-EMprimary cilia |
| spellingShingle | Raymond E Hulse Zongli Li Rick K Huang Jin Zhang David E Clapham Cryo-EM structure of the polycystin 2-l1 ion channel eLife PC-2L1 calcium TRP channel cryo-EM primary cilia |
| title | Cryo-EM structure of the polycystin 2-l1 ion channel |
| title_full | Cryo-EM structure of the polycystin 2-l1 ion channel |
| title_fullStr | Cryo-EM structure of the polycystin 2-l1 ion channel |
| title_full_unstemmed | Cryo-EM structure of the polycystin 2-l1 ion channel |
| title_short | Cryo-EM structure of the polycystin 2-l1 ion channel |
| title_sort | cryo em structure of the polycystin 2 l1 ion channel |
| topic | PC-2L1 calcium TRP channel cryo-EM primary cilia |
| url | https://elifesciences.org/articles/36931 |
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