Crystal Structure of the Eukaryotic Strong Inward-Rectifier K + Channel Kir2.2 at 3.1 Å Resolution
- 18 December 2009
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 326 (5960), 1668-1674
- https://doi.org/10.1126/science.1180310
Abstract
Bio-Diodes: Inward rectifier potassium channels conduct K + ions into the cell at internal negative membrane voltages, but at internal positive membrane voltages they are blocked by intracellular multivalent ions. These channels control the resting membrane voltage and are required for the healthy function of many electrically excitable cells. Mutations can result in transient paralysis causing, for example, heart problems. Tao et al. (p. 1668 ) now report a 3.1 angstrom resolution structure of the inward rectifier, Kir2.2 from chicken, which has a similar structure to the human equivalent. The combination of observations of conductive and inhibitory ion binding sites with electrophysiological data finally explains the mechanism of action of these long-studied channels and reveals how they maintain their low sensitivity to toxins, as well as provides a basis for the design of therapeutic drugs.Keywords
This publication has 64 references indexed in Scilit:
- Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environmentNature, 2007
- Crystal structure of a Kir3.1-prokaryotic Kir channel chimeraThe EMBO Journal, 2007
- The Role of the Cytoplasmic Pore in Inward Rectification of Kir2.1 ChannelsThe Journal of general physiology, 2007
- Crystal Structure of a Mammalian Voltage-Dependent Shaker Family K + ChannelScience, 2005
- The open pore conformation of potassium channelsNature, 2002
- Purification, Characterization, and Synthesis of an Inward-Rectifier K+ Channel Inhibitor from Scorpion VenomBiochemistry, 1997
- Anionic Phospholipids Activate ATP-sensitive Potassium ChannelsOnline Journal of Public Health Informatics, 1997
- An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantulaNeuron, 1995
- Control of rectification and permeation by residues in two distinct domains in an inward rectifier K+ channelNeuron, 1995
- A structural determinant of differential sensitivity of cloned inward rectifier K+ channels to intracellular spermineFEBS Letters, 1994