ArticleScience (New York, N.Y.)2009
Crystal structure of the eukaryotic strong inward-rectifier K+ channel Kir2.2 at 3.1 A resolution.
Article in Science (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 222 papers.
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Who cites it
222 citing papers in PubMed.
- Molecular mechanisms of Kir channel gating.Biochemical Society transactions · 2026Review
- Structural and functional studies of inward rectifier Kir7.1 and its regulation by the Melanocortin-4 receptor.Nature communications · 2026Article
- Potassium channels in vascular smooth muscle cells.Physiological reviews · 2026Review
- Cryo-EM structure of the human Kir7.1 channel reveals the molecular basis of snowflake vitreoretinal degeneration disease.Communications biology · 2026Article
- Repurposing polyamines to prevent life-threatening arrhythmias in Short QT Syndrome type 3.Nature communications · 2026Article
- Cryo-EM structures of heteromeric Kir4.1/5.1 channel suggest mechanisms of inward rectification and channel blockage.Nature communications · 2026Article
- Molecular architecture of the fungal-specific potassium channel TOK1.Nature communications · 2026Article
- Bioactive lipid-mediated structural and functional regulation of the essential human potassium channel Kir7.1.Nature communications · 2026Article
- Emerging methods for subtype differentiation in primary aldosteronism.Journal of internal medicine · 2026Review
- Direct crosstalk between GPCRs and ion channels via G proteins.Experimental & molecular medicine · 2025Review
- PIP2-driven cytoplasmic domain motions are coupled to Kir2 channel gating.The Journal of general physiology · 2025Article
- Kir6.2 channel activity is regulated by interaction of transmembrane domains 1 and 2 through I167 in the bundle-crossing gate.Physiological reports · 2025Article
- Genome-wide association analysis reveals insights into the genetic architecture of mesenteric torsion in pigs.Scientific reports · 2025Article
- Atomic-level investigation of KCNJ2 mutations associated with ventricular arrhythmic syndrome phenotypes.Scientific reports · 2025Article
- Review
- 3D-aligned tetrameric ion channels with universal residue labels for comparative structural analysis.Biophysical journal · 2025Article
- Article
- A phenylalanine at the extracellular side of Kir1.1 facilitates potassium permeation.Channels (Austin, Tex.) · 2024Article
- Detecting organelle-specific activity of potassium channels with a DNA nanodevice.Nature biotechnology · 2024Article
- Electro-metabolic signaling.The Journal of general physiology · 2024Article
162 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors.
Funding
Abstract
Inward-rectifier potassium (K+) channels conduct K+ ions most efficiently in one direction, into the cell. Kir2 channels control the resting membrane voltage in many electrically excitable cells, and heritable mutations cause periodic paralysis and cardiac arrhythmia. We present the crystal structure of Kir2.2 from chicken, which, excluding the unstructured amino and carboxyl termini, is 90% identical to human Kir2.2. Crystals containing rubidium (Rb+), strontium (Sr2+), and europium (Eu3+) reveal binding sites along the ion conduction pathway that are both conductive and inhibitory. The sites correlate with extensive electrophysiological data and provide a structural basis for understanding rectification. The channel's extracellular surface, with large structured turrets and an unusual selectivity filter entryway, might explain the relative insensitivity of eukaryotic inward rectifiers to toxins. These same surface features also suggest a possible approach to the development of inhibitory agents specific to each member of the inward-rectifier K+ channel family.
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Registered trials
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