Cryo-EM structure of the polycystin 2-l1 ion channel

Abstract
Data availability
Article and author information
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Abstract

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.

Data availability

The cryo map and model have been deposited to the Worldwide Protein Data Bank (6DU8) and Electron Microscopy Data Bank (8912).

The following data sets were generated

1. Clapham DE
2. Hulse RE
3. Li Z
4. Huang RK
5. Zhang J
(2018) Cryo map and model from
Publicly available at the Worldwide Protein Data Bank (Accession no: 6DU8).

http://www.wwpdb.org/
1. Clapham DE
2. Hulse RE
3. Li Z
4. Huang RK
5. Zhang J
(2018) Cryo map and model from
Publicly available at the Electron Microscopy Data Bank (Accession no: 8912).

https://www.ebi.ac.uk/pdbe/emdb/

The following previously published data sets were used

1. Shen
2. P.S.
3. Yang
4. X.
5. DeCaen
6. P.G.
7. Liu
8. X.
9. Bulkley
10. D.
11. Clapham
12. D.E.
13. Cao
14. E.
(2016) Cryo-EM structure of Polycystic Kidney Disease protein 2 (PKD2), residues 198-703
5T4D.

https://www.rcsb.org/structure/5T4D
1. Wilkes
2. M.
3. Madej
4. M.G.
5. Ziegler
6. C.
(2016) cryoEM Structure of Polycystin-2 in complex with calcium and lipids
5MKF.

https://www.rcsb.org/structure/5MKF
1. Wilkes
2. M.
3. Madej
4. M.G.
5. Ziegler
6. C.
(2016) cryoEM Structure of Polycystin-2 in complex with cations and lipids
5MKE.

https://www.rcsb.org/structure/5MKE

Article and author information

Author details

Raymond E Hulse

Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States

Competing interests
The authors declare that no competing interests exist.

"This ORCID iD identifies the author of this article:" 0000-0002-0110-3752
Zongli Li

Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, United States

Competing interests
The authors declare that no competing interests exist.
Rick K Huang

Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States

Competing interests
The authors declare that no competing interests exist.
Jin Zhang

Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States

Competing interests
The authors declare that no competing interests exist.
David E Clapham

Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States

For correspondence
claphamd@hhmi.org

Competing interests
The authors declare that no competing interests exist.

"This ORCID iD identifies the author of this article:" 0000-0002-4459-9428

Funding

Howard Hughes Medical Institute

David E Clapham

The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.

Copyright

This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.