Crystal structure of the human two-pore domain potassium channel K2P1 Journal Article


Authors: Miller, A. N.; Long, S. B.
Article Title: Crystal structure of the human two-pore domain potassium channel K2P1
Abstract: Two-pore domain potassium (K +) channels (K2P channels) control the negative resting potential of eukaryotic cells and regulate cell excitability by conducting K + ions across the plasma membrane. Here, we present the 3.4 angstrom resolution crystal structure of a human K2P channel, K2P1 (TWIK-1). Unlike other K + channel structures, K2P1 is dimeric. An extracellular cap domain located above the selectivity filter forms an ion pathway in which K + ions flow through side portals. Openings within the transmembrane region expose the pore to the lipid bilayer and are filled with electron density attributable to alkyl chains. An interfacial helix appears structurally poised to affect gating. The structure lays a foundation to further investigate how K2P channels are regulated by diverse stimuli.
Keywords: unclassified drug; protein conformation; protein analysis; cytology; amino acid sequence; molecular sequence data; protein multimerization; eukaryota; recombinant proteins; cell membrane; crystal structure; models, molecular; crystallography, x-ray; protein structure, tertiary; chemical structure; crystallization; protein structure, secondary; lipid bilayers; potassium; potassium ion; membrane potentials; ion channel gating; potassium channel; two pore pore domain potassium channel; potassium transport; potassium channels, tandem pore domain
Journal Title: Science
Volume: 335
Issue: 6067
ISSN: 0036-8075
Publisher: American Association for the Advancement of Science  
Date Published: 2012-01-27
Start Page: 432
End Page: 436
Language: English
DOI: 10.1126/science.1213274
PROVIDER: scopus
PUBMED: 22282804
DOI/URL:
Notes: --- - "Cited By (since 1996): 1" - "Export Date: 1 March 2012" - "CODEN: SCIEA" - "Source: Scopus"
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  1. Stephen Barstow Long
    34 Long
  2. Alexandria Miller
    10 Miller