Crystal structure of the human two-pore domain potassium channel K2P1 - PubMed (original) (raw)
. 2012 Jan 27;335(6067):432-6.
doi: 10.1126/science.1213274.
Affiliations
- PMID: 22282804
- DOI: 10.1126/science.1213274
Crystal structure of the human two-pore domain potassium channel K2P1
Alexandria N Miller et al. Science. 2012.
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.
Comment in
- Structural biology. The inner workings of a dynamic duo.
Poulsen H, Nissen P. Poulsen H, et al. Science. 2012 Jan 27;335(6067):416-7. doi: 10.1126/science.1217679. Science. 2012. PMID: 22282800 No abstract available. - Two-pore domain potassium channels: variation on a structural theme.
Braun AP. Braun AP. Channels (Austin). 2012 May-Jun;6(3):139-40. doi: 10.4161/chan.20973. Epub 2012 May 1. Channels (Austin). 2012. PMID: 22699405 Free PMC article.
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