Journal article
Crystal Structure of the Human Two-Pore Domain Potassium Channel K2P1
Science (American Association for the Advancement of Science), Vol.335(6067), pp.432-436
01/27/2012
DOI: 10.1126/science.1213274
PMID: 22282804
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.
Details
- Title: Subtitle
- Crystal Structure of the Human Two-Pore Domain Potassium Channel K2P1
- Creators
- Alexandria N. Miller - Memorial Sloan Kettering Cancer CenterStephen B. Long - Memorial Sloan Kettering Cancer Center
- Resource Type
- Journal article
- Publication Details
- Science (American Association for the Advancement of Science), Vol.335(6067), pp.432-436
- Publisher
- Amer Assoc Advancement Science
- DOI
- 10.1126/science.1213274
- PMID
- 22282804
- ISSN
- 0036-8075
- eISSN
- 1095-9203
- Number of pages
- 5
- Grant note
- Gerstner Young Investigator Award Burroughs Wellcome Career Award in the Biomedical Sciences; Burroughs Wellcome Fund
- Language
- English
- Date published
- 01/27/2012
- Academic Unit
- Molecular Physiology and Biophysics
- Record Identifier
- 9984446261302771
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