کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2030667 | 1071233 | 2007 | 9 صفحه PDF | دانلود رایگان |
SummaryPotassium channels fluctuate between closed and open states. The detailed mechanism of the conformational changes opening the intracellular pore in the K+ channel from Streptomyces lividans (KcsA) is unknown. Applying Monte Carlo normal mode following, we find that gating involves rotation and unwinding of the TM2 bundle, lateral movement of the TM2 helices away from the channel axis, and disappearance of the TM2 bundle. The open-state conformation of KcsA exhibits a very wide inner vestibule, with a radius ∼5–7 Å and inner helices bent at the A98–G99 hinge. Computed conformational changes demonstrate that spin labeling and X-ray experiments illuminate different stages in gating: transition begins with clockwise rotation of the TM2 helices ending at a final state with the TM2 bend hinged near residues A98–G99. The concordance between the computational and experimental results provides atomic-level insights into the structural rearrangements of the channel's inner pore.
Journal: - Volume 15, Issue 12, 13 December 2007, Pages 1654–1662