Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 407, Issue 2, Pages 366-371Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2011.03.025
Keywords
Allosteric regulation; Crystallography; Electrophysiology; G-protein; Inward rectifier K+ channel
Categories
Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan [20249012, 22136002]
- Grants-in-Aid for Scientific Research [22136001, 23590301, 22136002, 20249012] Funding Source: KAKEN
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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.
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