論文

査読有り
2011年4月

Inverse agonist-like action of cadmium on G-protein-gated inward-rectifier K+ channels

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
  • Atsushi Inanobe
  • ,
  • Takanori Matsuura
  • ,
  • Atsushi Nakagawa
  • ,
  • Yoshihisa Kurachi

407
2
開始ページ
366
終了ページ
371
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1016/j.bbrc.2011.03.025
出版者・発行元
ACADEMIC PRESS INC ELSEVIER SCIENCE

The gate at the pore-forming domain of potassium channels is allosterically controlled by a stimulus-sensing domain. Using Cd2+ as a probe, we examined the structural elements responsible for gating in an inward-rectifier K+ channel (Kir3.2). One of four endogenous cysteines facing the cytoplasm contributes to a high-affinity site for inhibition by internal Cd2+. Crystal structure of its cytoplasmic domain in complex with Cd2+ reveals that octahedral coordination geometry supports the high-affinity binding. This mode of action causes the tethering of the N-terminus to CD loop in the stimulus-sensing domain, suggesting that their conformational changes participate in gating and Cd2+ inhibits Kir3.2 by trapping the conformation in the closed state like "inverse agonist". (C) 2011 Elsevier Inc. All rights reserved.

Web of Science ® 被引用回数 : 8

リンク情報
DOI
https://doi.org/10.1016/j.bbrc.2011.03.025
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/21396912
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000289746700018&DestApp=WOS_CPL

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