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Science (American Association for the Advancement of Science), 2009-12, Vol.326 (5960), p.1668-1674
2009

Details

Autor(en) / Beteiligte
Titel
Crystal Structure of the Eukaryotic Strong Inward-Rectifier K+ Channel Kir2.2 at 3.1 Å Resolution
Ist Teil von
  • Science (American Association for the Advancement of Science), 2009-12, Vol.326 (5960), p.1668-1674
Ort / Verlag
Washington, DC: American Association for the Advancement of Science
Erscheinungsjahr
2009
Link zum Volltext
Quelle
Science Online_科学在线
Beschreibungen/Notizen
  • 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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