The pore structure of the closed RyR1 channel
The pore structure of the closed RyR1 channel
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DOI：
10.1016/j.str.2005.06.005
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发表时间：
2005-08-01
期刊：
影响因子：
5.7
通讯作者：
Chiu, W
中科院分区：
文献类型：
--
作者：
Ludtke, SJ;Serysheva, II;Chiu, W
使用单粒子电子冷冻显微镜，几个螺旋在跨膜区域的RyR1，包括一个内部跨膜螺旋，一个短孔螺旋，和一个螺旋平行于细胞质侧的膜，已清楚地解决。我们的模型将高度保守的甘氨酸（G4934）放置在弯曲的内螺旋的铰链位置，并在孔的管腔和细胞质口处放置两个负电荷环。扭结的内螺旋与开放的MthK通道的内螺旋非常相似，这表明单独的扭结不会打开RyR1，正如K通道所提出的那样。
Using single particle electron cryomicroscopy, several helices in the membrane-spanning region of RyR1, including an inner transmembrane helix, a short pore helix, and a helix parallel to the membrane on the cytoplasmic side, have been clearly resolved. Our model places a highly conserved glycine (G4934) at the hinge position of the bent inner helix and two rings of negative charges at the luminal and cytoplasmic mouths of the pore. The kinked inner helix closely resembles the inner helix of the open MthK channel, suggesting that kinking alone does not open RyR1, as proposed for K channels.