IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v413y2001i6858d10.1038_35101535.html
   My bibliography  Save this article

Ion conduction pore is conserved among potassium channels

Author

Listed:
  • Zhe Lu

    (University of Pennsylvania)

  • Angela M. Klem

    (University of Pennsylvania)

  • Yajamana Ramu

    (University of Pennsylvania)

Abstract

Potassium channels, a group of specialized membrane proteins, enable K+ ions to flow selectively across cell membranes. Transmembrane K+ currents underlie electrical signalling in neurons and other excitable cells. The atomic structure of a bacterial K+ channel pore has been solved by means of X-ray crystallography. To the extent that the prokaryotic pore is representative of other K+ channels, this landmark achievement has profound implications for our general understanding of K+ channels. But serious doubts have been raised concerning whether the prokaryotic K+ channel pore does actually represent those of eukaryotes. Here we have addressed this fundamental issue by substituting the prokaryotic pore into eukaryotic voltage-gated and inward-rectifier K+ channels. The resulting chimaeras retain the respective functional hallmarks of the eukaryotic channels, which indicates that the ion conduction pore is indeed conserved among K+ channels.

Suggested Citation

  • Zhe Lu & Angela M. Klem & Yajamana Ramu, 2001. "Ion conduction pore is conserved among potassium channels," Nature, Nature, vol. 413(6858), pages 809-813, October.
    • Handle: RePEc:nat:nature:v:413:y:2001:i:6858:d:10.1038_35101535
    DOI: 10.1038/35101535
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/35101535
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/35101535?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Gamma Chi & Qiansheng Liang & Akshay Sridhar & John B. Cowgill & Kasim Sader & Mazdak Radjainia & Pu Qian & Pablo Castro-Hartmann & Shayla Venkaya & Nanki Kaur Singh & Gavin McKinley & Alejandra Ferna, 2022. "Cryo-EM structure of the human Kv3.1 channel reveals gating control by the cytoplasmic T1 domain," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    2. Georg Kuenze & Amanda M Duran & Hope Woods & Kathryn R Brewer & Eli Fritz McDonald & Carlos G Vanoye & Alfred L George Jr. & Charles R Sanders & Jens Meiler, 2019. "Upgraded molecular models of the human KCNQ1 potassium channel," PLOS ONE, Public Library of Science, vol. 14(9), pages 1-33, September.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:413:y:2001:i:6858:d:10.1038_35101535. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.