Three-dimensional rearrangements within inositol 1,4,5-trisphosphate receptor by calcium
Three-dimensional rearrangements within inositol 1,4,5-trisphosphate receptor by calcium
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DOI：
10.1074/jbc.m309743200
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发表时间：
2003-12-26
影响因子：
4.8
通讯作者：
Mikoshiba, K
中科院分区：
文献类型：
--
作者：
Hamada, K;Terauchi, A;Mikoshiba, K
钙离子（Ca2+）与肌醇1,4,5-三磷酸（IP3）受体（IP3R）的变构结合控制IP3R内的通道门控。在这里，我们提出了生物化学和电镜证据Ca2+敏感的结构变化在1型IP3R （IP(3)R1）的三维结构。低浓度的Ca2+和高浓度的Sr2+和Ba2+对IP(3)R1的有限蛋白水解有效，但Mg2+对蛋白质水解没有影响。电镜和有限的蛋白水解一致表明，Ca2+对IP(3)R1构象变化的有效浓度为
Allosteric binding of calcium ion (Ca2+) to inositol 1,4,5-trisphosphate (IP3) receptor (IP3R) controls channel gating within IP3R. Here, we present biochemical and electron microscopic evidence of Ca2+-sensitive structural changes in the three-dimensional structure of type 1 IP3R (IP(3)R1). Low concentrations of Ca2+ and high concentrations of Sr2+ and Ba2+ were shown to be effective for the limited proteolysis of IP(3)R1, but Mg2+ had no effect on the proteolysis. The electron microscopy and the limited proteolysis consistently demonstrated that the effective concentration of Ca2+ for conformational changes in IP(3)R1 was