IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v410y2001i6832d10.1038_35074145.html
   My bibliography  Save this article

Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin

Author

Listed:
  • Maria A. Schumacher

    (Vollum Institute, Oregon Health Sciences University)

  • Andre F. Rivard

    (Vollum Institute, Oregon Health Sciences University)

  • Hans Peter Bächinger

    (Shriners Hospital for Children, Research Unit
    Oregon Health Sciences University)

  • John P. Adelman

    (Vollum Institute, Oregon Health Sciences University)

Abstract

Small-conductance Ca2+-activated K+ channels (SK channels)1,2 are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming α-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through the CaM-binding domain (CaMBD), which is located in an intracellular region of the α-subunit immediately carboxy-terminal to the pore3,4. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM4. Here we report the 1.60 Å crystal structure of the SK channel CaMBD/Ca2+/CaM complex. The CaMBD forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three α-helices, two from one CaMBD subunit and one from the other. As only the CaM N-lobe has bound Ca2+, the structure provides a view of both calcium-dependent and -independent CaM/protein interactions. Together with biochemical data, the structure suggests a possible gating mechanism for the SK channel.

Suggested Citation

  • Maria A. Schumacher & Andre F. Rivard & Hans Peter Bächinger & John P. Adelman, 2001. "Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin," Nature, Nature, vol. 410(6832), pages 1120-1124, April.
    • Handle: RePEc:nat:nature:v:410:y:2001:i:6832:d:10.1038_35074145
    DOI: 10.1038/35074145
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/35074145
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/35074145?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. Massimo Lai & Denis Brun & Stuart J Edelstein & Nicolas Le Novère, 2015. "Modulation of Calmodulin Lobes by Different Targets: An Allosteric Model with Hemiconcerted Conformational Transitions," PLOS Computational Biology, Public Library of Science, vol. 11(1), pages 1-28, January.
    2. Harris E. Blankenship & Kelsey A. Carter & Kevin D. Pham & Nina T. Cassidy & Andrea N. Markiewicz & Michael I. Thellmann & Amanda L. Sharpe & Willard M. Freeman & Michael J. Beckstead, 2024. "VTA dopamine neurons are hyperexcitable in 3xTg-AD mice due to casein kinase 2-dependent SK channel dysfunction," Nature Communications, Nature, vol. 15(1), pages 1-20, December.

    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:410:y:2001:i:6832:d:10.1038_35074145. 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.