1. Structural Biology and Molecular Biophysics
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Cryo-EM structure of the polycystin 2-l1 ion channel

  1. Raymond E Hulse
  2. Zongli Li
  3. Rick K Huang
  4. Jin Zhang
  5. David E Clapham  Is a corresponding author
  1. Howard Hughes Medical Institute, United States
  2. Harvard Medical School, United States
Research Article
  • Cited 27
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Cite this article as: eLife 2018;7:e36931 doi: 10.7554/eLife.36931

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

Article and author information

Author details

  1. Raymond E Hulse

    Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States
    Competing interests
    The authors declare that no competing interests exist.
    ORCID icon "This ORCID iD identifies the author of this article:" 0000-0002-0110-3752

  2. 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.

  3. Rick K Huang

    Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States
    Competing interests
    The authors declare that no competing interests exist.

  4. Jin Zhang

    Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States
    Competing interests
    The authors declare that no competing interests exist.

  5. 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.
    ORCID icon "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.

Reviewing Editor

  1. Baron Chanda, University of Wisconsin-Madison, United States

Publication history

  1. Received: March 23, 2018
  2. Accepted: July 12, 2018
  3. Accepted Manuscript published: July 13, 2018 (version 1)
  4. Version of Record published: July 23, 2018 (version 2)

Copyright

© 2018, Hulse et al.

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.

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