Corrigendum.

Abstract

CorrigendumCorrigendumPublished Online:14 Sep 2016https://doi.org/10.1152/physrev.z9j-2787-corr.2016Original articleMoreSectionsPDF (109 KB)Download PDF ToolsExport citationAdd to favoritesGet permissionsTrack citations ShareShare onFacebookTwitterLinkedInWeChat Volume 95, January, 2015Sepúlveda FV, Cid LP, Teulon J, Niemeyer MI. Molecular aspects of structure, gating, and physiology of pH-sensitive background K2P and Kir K+-transport channels. Physiol Rev 95: 179–217, 2015. doi: https://doi.org/10.1152/physrev.00016.2014.There is an error in the distribution of transmembrane domains in the bottom right of FIGURE 1A.The corrected figure is printed below.FIGURE 1.A: topological model for two-pore-domain potassium (K2P) channel subunit (top: shown in side view with the membrane in gray). Each subunit is made of four transmembrane segments, TM1-TM4, and two pore-forming domains, P1 and P2. P domains penetrate partially into the membrane. A thicker portion represents the selectivity filter. The SID (self-interacting domain) is a large extracellular loop often making contact with its partner in the other subunit of the channel through a disulfide bridge. Two subunits associate to form a dimer with bilateral symmetry and pseudo-fourfold symmetry around the pore as shown in the bottom diagrams (seen from the extracellular side looking into the membrane). Two alternative forms of association of transmembrane domains are shown. The one on the left corresponds to that revealed by the first two X-ray structures of K2P channels and the one on the right to what has been termed a domain-swapped configuration (see text for further description of these) where outer helices are exchanged between protomers. P1 and P2 domains contribute to the pore with identical P domains facing each other diagonally across the permeation pathway. B: topological model for inwardly rectifying K+ (Kir) channel subunit (top) with the organization of tetramers illustrated at the bottom. Other details as in A. C: schematic depiction of K+ channel KcsA structure. Two of the four subunits of this two-TM homotetramer pore are shown with the extracellular side on top. Each subunit contains an outer helix (helices shown as boxes) close to the membrane, an inner helix close to the pore, a short pore helix, and a selectivity filter (SF, thick line). K+ ions are shown as gray spheres along the pore. Accompanying water molecules have been omitted. [Based on MacKinnon (245).]Download figureDownload PowerPointThis article has no references to display. Download PDF Previous Back to Top FiguresReferencesRelatedInformation Related ArticlesMolecular Aspects of Structure, Gating, and Physiology of pH-Sensitive Background K2P and Kir K+-Transport Channels 01 Jan 2015Physiological Reviews More from this issue > Volume 96Issue 4October 2016Pages 1665-1665 Copyright & PermissionsCopyright © 2016 the American Physiological Societyhttps://doi.org/10.1152/physrev.z9j-2787-corr.2016PubMed27630178History Published online 14 September 2016 Published in print 1 October 2016 Metrics