3ukm

Publication Abstract from PubMed

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.

Crystal structure of the human two-pore domain potassium channel K2P1.,Miller AN, Long SB Science. 2012 Jan 27;335(6067):432-6. PMID:22282804^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.