Structural Diversity in the Cytoplasmic Region of G Protein-Gated Inward Rectifier K<SUP>+</SUP> Channels

DOI
  • Inanobe Atsushi
    Div. of Mol. and Cell. Pharmacol., Dept. of Pharmacol., Grad. Sch. of Med., Osaka Univ.
  • Kurachi Yoshihisa
    Div. of Mol. and Cell. Pharmacol., Dept. of Pharmacol., Grad. Sch. of Med., Osaka Univ.

Bibliographic Information

Other Title
  • G蛋白質制御内向き整流性カリウムチャネルの細胞質領域における構造的多様性

Abstract

Inward rectifier K+ (Kir) channels can be functionally categorized into two groups: those that are constitutively active and those that are constitutively inactive, with examples such as Kir2.x and Kir3.x, respectively. Their cytoplasmic regions are thought to be critical for control of channel gating, but a structural basis for this hypothesis is not known. In this study, we report a structure for the cytoplasmic region of a G protein-gated Kir channel, Kir3.2, and compare it with those of Kir3.1 and Kir2.1 channels. The isolated cytoplasmic region of Kir3.2 forms a tetrameric assembly in solution and also in the crystal. While the secondary structure arrangement and the subunit interface of the Kir3.2 crystal structure are found to be nearly identical to those of Kir3.1 and Kir2.1, it is quite different at and around loops between βC- and βD-strands and between βH- and βI-strands. These structural elements are located at the interface with the plasma membrane and therefore could associate with the Kir channel transmembrane helices. These structural elements could therefore be involved in the regulation of Kir channel gating. [J Physiol Sci. 2007;57 Suppl:S232]

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Details 詳細情報について

  • CRID
    1390282680705723520
  • NII Article ID
    130005449261
  • DOI
    10.14849/psjproc.2007.0_232_2
  • Data Source
    • JaLC
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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